two-color stereo diagrams -...

APPENDIX

Two-Color Stereo Diagrams

APPENDIX


Plate I. II.

I II A. III B. IV. V.

VI. VII.

VIII. IX. X.

XI. XII.

XIII. XIV. XV.

XVI. XVII.

XVIII. XIX A. XIX B. XX.

XXI. XXII.

XXIII. XXIV A. XXIV B.

XXV. XXVI.

XXVII. XXVIII.

XXIX.

LIST OF STEREO DIAGRAMS

Chymotrypsin Ay inhibited by AAAPCK Acylation of Chymotrypsin Ay a-Chymotrypsin complex with N-formyl-tryptophan a-Chymotrypsin Active Site Subtilisin Active Site Acetyl Ala-Gly-Phe Chloroketone DIP-Trypsin :c-carbons Trypsin Active Site ~-Chymotrypsin a-carbons Elastase Polypeptide Chain Pancreatic Trypsin Inhibitor Binding Site of UpcA to Ribonuclease-S Staphylococcal Nuclease Peptide Chain, view from front Staphylococcal Nuclease Peptide Chain, view from right Staphylococcal Nuclease Peptide Chain, view from top Binding of pdTp and Ca ++ to Staphylococcal Nuclease Human Carbonic Anhydrase C a-carbons Human Carbonic Anhydrase C Active Site Carboxypeptidase Peptide Chain Carboxypeptidase Active Site Binding of Gly-Tyr to Carboxypeptidase Rhombohedral 2 Zinc Insulin, view perpendicular to 3-fold axis H-Bonding between Molecules in Insulin Dimer Lysozyme "Inhibitor and Its Electron Density Lysozyme Inhibitor and Active Site of Lysozyme /~ C-terminal Region of Deoxyhemoglobins A and Rainier fl C-terminal Region of Deoxyhemoglobins A (top) and Rainier, view toward 2-fold

axis Cytochrome b 5 a-carbons, view parallel to c axis Cytochrome b 5 a-carbons, view perpendicular to c axis Horse Heart Ferricytochrome c Lactate Dehydrogenase a-carbons Lactate Dehydrogenase Active Site

595

596 P L A T E L E G E N D S

I. Chymotrypsin Ay inhibited by AAAPCK. Only the port ion of the enzyme which may interact with the inhibitor has been shown.

I I . Proposed enzyme-ester intermediate showing AAAP acylat ing Ser 195 of chymotrypsin A~.

I I I A . Active site :region of the complex of crystalline ~-chymotrypsin with formyl-L-tryptophan.

I I I B. Active site region of ~-chymotrypsin, ro ta ted to match the active site region of subtilisin as shown in Pla te IV.

IV. Active site :region of subtilisin BPI~'.

V. Active site region of subtilisin with the inhibitor acetyl-L-A]a.Gly-L-Phe methylene bound to Ne 2 of His 64.

VI. Positions of the a-carbons in DIP- t ryps in . Side chains of the most impor tant catalyt ic groups and cystine bridges are included. The DIP- inhibi tor has been removed for clar i ty and the y-oxygen of Ser 195 is in the position found in the inhibited molecule.

The following three plates have been rota ted to match the orientation of DIP- t ryps in for comparison.

VI I . Act ive site region of DIP- t ryps in . Numbering of the ~-carbon positions follows the chymotrypsinogen A scheme. Some important catalyt ic side chains and hydrogen bonds are also shown. The D I P group has been left out for clarity, and a rotat ion about the ~-fl bond of Ser 195 has beea performed to set up the ant ic ipated H-bond arrangement in the nat ive enzyme.

VI I I . ~-Carbon positions and folding of the polypept ide chain in nat ive cr Side chains of the most impor tant catalyt ic groups and cystine bridges are also shown.

IX. Folding of the polypept ide chain in elastase. The co-carbons are shown together with eystine bridges.

X . Positions of the main chain Ca, C, O and N atoms of pancreatic t rypsin inhibitor. H-bonds are indicated by dot ted lines. Circles enclosing the amino acid numbers are at the positions of the Ca carbons. Disulfide bridges are heavily outlined. The twisted fl-structure from 16 to 36 can be seen. The reactive site a t Lys 15 is very exposed at the top of the molecule.

XI . The binding of UpcA to ribonuclease-S. Only those parts of the protein in the vicinity of the dinueleotide are shown.

X I I . Staphylococcal nuclease, view of the pept ide chain from the front.

X I I I . Staphylococcal nuclease, view of the pept ide chain from the right.

XIV. Staphylococcal nuclease, view of the peptide chain from the top.

XV. Detailed view of the binding of the thymidine-3 ' , 5 ' -diphosphate inhibitor and Ca ++ to staphylococcal nuclease.

XVI. ~-Carbon atoms of human carbonic anhydrase C.

XVII . Human carbonic anhydrase C, some residues surrounding the zinc ion and two hist idyl residues further out in the active site.

X V I I I . Polypept ide chain of the entire carboxypept idase molecule.

X I X A. One-quarter of the CPA molecule, showing active site region. The remainder of the protein continues be,low and to the left of the fl-structure on the left.

X I X B. The same region of CPA after glycyl-L-tyrosine is bound (heavy circles) and after conformation changes have occurred for residues Arg 145, Glu 270 and Tyr 248 (solid discs).

XX. Rhombohec[ral 2 zinc insulin, view perpendicular to 3-fold axis.

PLATE LEGENDS 597

XXI. H-bonding between the N-terminal extended chains in the insulin dimer, viewed along the local monomer-monomer 2-fold axis.

XXII .

X X I I I .

X X l V A.

XXIV B.

XXV.

XXVI.

XXVII .

XXVII I .

XXIX.

Difference electron-density map of aspartamido-N-acetylglucosamine bound to lysozyme. For purposes of reproduction, this figure has been prepared from a copy on an incremental plotter of the original C.R.T. image.

Active site region of lysozyme showing the binding of aspartamido-N-acetylglucosamine.

fl C-terminal region of normal deoxyhemoglobin (. ) and deoxyhemoglobin Rainier (- - -). Bold lines indicate the main chains, light ones the side chains.

fl C-terminal area of normal deoxyhemoglobin (top) and deoxyhemoglobin Rainier, viewed from outside the molecule looking in towards the molecular twofold axis. The heine group is represented by a line since it is parallel to the direction of view.

~-Carbon chain of cytochrome bs, view parallel to c axis.

~-Carbon chain of cytochrome bs, view perpendicular to c axis.

Backbone of the horse heart ferricytochrome c molecule. In this orientation, the top of the molecule as seen in Fig. 1 of Takano et ah (this volume) has been tipped forward 70 ~ about a horizontal axis. Only the a-carbon backbone, the heine, and certain key side chains are shown. Phe 46 is drawn as tyrosine, with its oxygen atom as in tuna and bonito cytochrome c.

~-Carbon positions of one subunit of lactate dehydrogenase, viewed from the molecular center along c.

Active site region of lactate dehydrogenase showing the coenzyme and the suggested position of lactate ion and residues which may be important for binding and reaction.

�9

0 . Oo CT$~O

C'fSlgt

RE'I'I92

I=lSlPtSq

'1R219

PIE PI

SER195

SEl~lq

SER21"/

61.1'216

RLR I~

NI$

I~ Pq

RU=I 1=3

O~c

0 ~

O~ bS

CTS~L~?

~,I~ �84184 /,/

YYHB2z9

SEA217

GL~I6

ACA P3

;PW

iPHE P1

; , ~ 9 5

, ~H11i:!57

PL ,\"F E I I~

v t93

his $7 ser lg5

H r 214 set 189

cys 220

thrLPl9

~:~N

�9

t rp 215 gly 216

SEB ] 90

P3 p ~ 9~

/}/

bIET . ]

<: y 193 ~ L :

SER 189 �9 CAR~@N @ NIIROGCN Q O• G SUL_FUR

OLY 216 '~

(1~ ~ sen 21~

/

2E~ 1~95 ~

HIS 57

/

102

PLKTE I I IB

flLA

THR 220

GLY 219

I:FISN

SEB 221 ~

s~ CARBON

@ NITR@SEN

�9 OXYSEN

GkY 127~

155 ~ ,:v ~"0

/ SER 33

~ HIs 6~ ~%

ALA 153

CASBON

@ NITROGEN 0 OXYGEN

GLY 1 2 7

THA 22O i

ALA 152

PHE P_I 155 ~ .... SEA t 25

GLY ~

U 126

TTL pu~

ALA P3

GLT 219 SER 221

,I

ASP 32

HIS 6E

~ 5 E R 33

~ I ~ Q o Q I

O O O e 0 0

m 0 o o 0 ~ 0

Q B o

W

B i

o D

Q I

Q

o

Q

o

o f ,

I

U

0 a

0

o

O o

o D

i

l

~ J

,p

!

~ ~ ~ 7 ~

a.

f /

86 36

C~

C

] .

LJ

L3

J

100 110

250

90

LEU HIS 95

198 197

HIS 63

HIS 93 HIS I I~E u 196

GLX 66

HIS 128

i,r,i~

)Sa

I m

d

130

129

TI-IR

GLY 1

PHE

6LY 10e

121

CYS

8

CY:

!0

10

ALA

117

HIS .105

11 03

PIlE 101

d

J f

,J TYR

PHE PHE

)

ARG 45

• '--, , ' ~ 63 /

!

SER C(~

SM

, _ ^ . , ', / " 5 8 t"& ~. F-I ~ I'1 ,.,-., ( '~ I

/ I

[ n s N O,

GLM 57

43

98

. ALA~

. - ' ~ 108

0,1 56 ~

d., G ~ L ~ 110 b

ASP 101

99

GLY 102

ASM 103

l l m > ' i �9

~ L I �84

1 , N

U

L .

Z

=

>'l 0

"k \

"<\

i ',~ U I,,I1~ .... (,~ l i .

( J Z 0 (/)

o0@O

./

Cys F9

J J

Tyr HC2 rHiS ,F8

I-lts~HC3~' Asp FG1

~C ON �9 �9

~ , C,s F9

_~ His !F8 Cys HC2 ~ /

Asp FG1 ~ /

cO

Z LJ

>-

b~

L.~_i

C9

!-

~ 4 ~,

SUBJECT INDEX

A

Acetyl CoA-arylamine acetyltrans- ferase, 7

Acetylimidazole, 3 Acid-base catalysis, 1-11, 61, 66 Actinomycin, 263-270 Actinomycin-DNA complex

medical implications of stereochemical model, 269

proposed structure, 266-268 Actinomycin-DNA interaction, solu-

tion studies, 263-264 Actinomycin-deoxyguanosine crystal-

line complex, 263-270 dyad axis in actinomycin and com-

plex, 264-265 Active center topography during ca-

talysis, 527-529 Active site

aspartate transcarbamylase, 289 carbonic anhydrase, 226-229 carboxypeptidase A, 562 chymotrypsin, 63-65 comparison of trypsin with other

serine proteases, 133-135 elastase, 95 lactate dehydrogenase, 186-188 phosphoryl-transferring enzymes,

533-540 ribonuclease-S, 40-42 spectral probes, 519-521 staphylococcal nuclease, 248-249 subtilisin, 109-110, 119 triose phosphate isomerase, 153-154 trypsin, 130, 134, 138-139

Acyl a-chymotrypsin, 64, 74-83 Acylamide ester substrates of chymo-

trypsin, 80-83 Adenovirus hexon, 503-509

Patterson map, analysis of, 505-506 physical and chemical properties of,

5O4-5O5 precession photographs, analysis of,

507-509 Adenylate kinase, 538-539 Aldolase, 160 Alakaline phosphatase, from E. coli,

520-521 Allosteric

hemoglobin model, 337-341 proteins, 193-198, 285-290

Aminolysis, 3-4 Anhydride, 24-25 Anilides, 5-6

Anomalous dispersion, 382 Antibodies, 413-419, 421-425, 427-432 Applications of X-ray studies, 591-592 Approximation, role in catalysis, 25-

26 Arsanilazoprocarboxypeptidase, 523-

525 Arsanilazochymotrypsinogen, 522

o-arylacryloyl-chymotrypsins, 76-80 Aspartate aminotransferase, 517-518 Aspar tokinase-l-homoserine dehydro-

genase, 193-198 relaxations of coenzyme binding to,

196-197 slow relaxation, 194-196

Aspartate transcarbamylase, 285-290 crystal forms and molecular symme-

try, 285 data collection and refinement, 287-

288 electron-density map at 5.5 3, resolu-

tion, 288-290 snbunit structure from electron-

density map, 289 Azochromophores, 522

B

B12-dependent enzyme, 60 Bence-Jones protein, 427-432 Bijvoet difference Fourier map, 371,

383 Bohr effect, 302-306, 315

C-terminal residues, tests of role, 303-307

Bond rotation, effect on catalysis, 25

C

Calcium-binding protein, 217-220 strncture interpretation, 219-220

Calcimn ion, 217-220, 243-245, 271 Carbonic anhydrase, 221-231

active site, 226-229 comparisons with available chemical

sequences, 223-225 description of molecular structure,

221-223 inhibitor complexes, 227-229 side-chain location, 225-226 solvent molecules in the active site,

229 zinc coordination, 226-227

Carboxypeptidase A, 519-520, 551-558, 561-566

esterase activity, 565-566 L- and D-phenylalanine inhibition,

564-565 Mg-CPA, proton relaxation studies

of, 553-557 Mn ++ substitution, 551

NMR dispersion, results, 563-566 pH effects in CPA, 566 substrate binding to Mn-CPA, 565

Carboxypeptidase S, 523-524 Catalysis, 1-33, 45-70, 75-83

bond rotation, 25 charge relay system, 9, 67, 94-96, 117,

134, 189 enzyme strain, 53-62, 66 general acid-base, 1-10, 61, 66 orientation, 13-27, 66 proximity, 13-27, 66 substrate strain, 29-33, 45-51, 66 X-ray diffraction methods of study,

63-70 Cation binding site in subtilisin, 109

Cell organelles, 590 Charge relay system, 9

in chymotrypsin, 67 in elastase, 94-96 in lactate dehydrogenase, 189 in subtilisin, 117 in trypsin, 134

Chemical catalysis, 66 Chemical intermediates, 66 Chloromethyl ketones

subtilisin binding of, 117-120 Chromatium iron protein, 381-385 Chymotrypsin, 2, 4, 5-8, 9-10, 63-90

acyl a-chymotrypsin, 64 binding of chloromethyl ketones to

3' crystals, 85-88 comparison of A and A a structures,

85 comparison with elastase, 99-101 comparison with subtilisin, 120-123 comparison with trypsin, 131-134 conformation equilibria and the salt

bridge in, 71-73 interaction with substrate analogs,

63-65 kinetic consequences of substrate

binding scheme, 88-90 spectrophotometric studies of acyl

derivatives of, 75-83 structure of active center, 63-65

634 SUBJECT INDEX

Chymotrypsin (continued)

structure of acyl intermediate, 88 substrate binding site, comparison

with elastase, 99-101 substrate binding site of subtilisin

resemblance to chymotrypsin, 121-123

substrate analog binding to a, 85-90 7, 63-65

transition state analogs of substrate for, 47-48

X-ray diffraction studies of a, 63-70 7, 85-90

a-Chymotrypsin, 63-70 7-Chymotrypsin, 85-90 Chymotrypsinogen, 122 Chymotrypsinogen A, 522

Circular dichroic changes, chemical basis of, 526-527

Circular dichroism, 520

Comparison of subtilisin BPN' and subtilisin Novo, 107-116

method of, 108

Complexes of lactate dehydrogenase with coenzyme, 183-184

Computer-controlled display system, 577-583

electron density representation, 580 of molecular models, 578

Concanavalin A, 271-284 electron-density maps at 3 A, 275 electron-density map at 4 A, 274,

280-281 Conformation of arsanilazocarboxy-

peptldase in the crystalline state and in solution, 524-527

Conformational changes, 522-523 m carhoxypeptidase upon substrate

binding, 526, 561-562 m cytochrome c upon oxidation,

397-404, 409-410 in elastase upon inhibi tor binding

to, 99 m hemoglobin upon oxygenation of

deoxy-, 295-300, 546-549 m LDH on binding NAD § and! pyru-

vate, 186 m lysozyme binding trifluoroacety-

lated analog of chitotriose, 541- 544

in riboquclease-S selectively trifluoroacetylated, 544-546

Conformational effects in selectively trifluoroacetylated hemoglobin A, 546-549

Cooperativity, 311-314 concerted transition model, 331 models for hemoglobin, 331-335 role of salt bridges, 307

Cooperativity (continued)

sequential model, 331-332 C.P.K. models, 585-586 Creatine kinase, 536-538

internuclear distances in the active complex, 536

model of topography of substrate at active site of, 537

Crystal vs. solution structure and activity

�9 7-chymotrypsin, 88-90 elastase, 92-94 hemoglobin, 308-309 spectro-chemical probes of, vs. na-

tive enzyme, 524-527 Crystallization, 590

effect on molecular structure of hemoglobin, 308-309

micro-diffusion cells, use of, 291 of trypsin-pancreatic trypsin inhibi-

tor complex, 148-149 Cytochrome bs, 387-395

comparison of structure with cytochrome c and myoglobin, 393

iron ligands in, 393 Cytochrome c, 59, 397-411

conformational changes upon oxidation, 399-402, 409-410

electron transfer, kinetics of, 407 sixth ligand, 398-399 trigger mechanism, 402 Winfield mechanism, 402

Cytochrome oxidase binding to cytochrome c, 402

D

Dansyl fluorescence, 527-529 Degrees of freedom, translational and

rotational, 21

Dehydrogenases, 171-203 aspartokinase-I-homoserine dehydro-

genase, 193-198 glyceraldehyde-phosphate, 167 t~-ketoglutarate, 199-203 lactate, 179-191 malate, 171-178

Denaturation-renaturation of S. nuclease

kinetic studies, 251 NMR studies, 251

Densitometer, 217 computer-controlled, 436

Deoxyrihonuclease, 268

Desolvation, 24

Diazonium salts, 522 Diazotised arsanilic acid, 524-525 Difference Fourier, structure determi-

nation of small metabolites by, 101-103

Di-isopropyl trypsin, 125-132 2,3-Diphosphoglycerate, 325 Divergent evolution, 132-133, 353

E

Elastase catalytic activity of crystals, 92-94 crystalline inhibitor-elastase com-

plexes minor binding site at active site,

99 preparation of, 97-98 structure of, 98-100

differences between tosyl- and native, 94

inhibit ion by a sulfonyl fluoride de- rivative of glutathione, 102

inhibit ion by tosyl fluoride, 91 inhibitor binding, 91-105 NMR studies of, 95-96 specificity towards ester and peptide

substrates, 96-97 structure and homologies, 91 structure of native enzyme at pH 5.0

and 8.5, 94-96 substrate analog binding site, com-

parison with chymotrypsin, 99- 101

use of crystalline elastase for structure determination of small molecules, 101-103

X-ray diffraction studies of, 91-105 Electron density, computer display

representation of, 580 Electronic contributions to absorption

spectra of strong chromophores, 76-78

Electron micrographs, interpretation of, 489

Electron microscopy, 199-203, 590 of adenovirus hexon "groups of

nine," 507-508 of crystalline enzymes, 199-200 of immunoglobin, 413-419 of immunoglobulin crystals, 414 interpretation of, 489-490 three-dimenslonal image reconstruc-

tion, 489-494 of TMV

partially reconstituted, 463 protein disks, 452

Electron transfer in cytochrome c, 403 proteins, 58-61

Electron transport, 387 Enolase, 169-170 Entatic state, 53-62 Entropy of activation, 21 Enzyme specificity, serine proteases,

131

SUBJECT INDEX 635

Enzyme-substrate complexes, 591 carboxypeptidase, 561

Esterase, 5

F

Ferredoxln, 60 Ferricytochrome c, 397 Finkelstein reaction, 23-24 Flavodoxin, 369-379

flavin, 369 isoallosazine ring, 376 oxidation-reduction potential, 369 semiquinone structure at 3.25 A,

371-376 semiquinone and oxidized structures

compared, 376-378 semiquinone radical, 369

Flavoprotein, 369-379 FMN, 369 agF-NMR spectroscopy, 541-549

G

Gamma rays, 511-516 Glutamine synthetase, 291-294

molecular symmetry of, 293-294 Glutathione, structure when attached

to elastase, 103 Glycolytic pathway, X-ray studies on

enzymes in, 165-170 Guanidinium ion of arginine, 249

H

Heavy atom derivatives, 272, 590 aspartate transcarbamylase, 285-286 calcium-binding protein from carp

muscle, 217-218 carbonic anhydrase, 221 concanavalin A, 278 cytochrome bs, 387-388 cytochrome c, 398 flavodoxin, 370, 377 immunoglohulin, 413-414, 428~129 immunoglobulin Fab and Fc frag-

ments, 421-424 lactate dehydrogenase, 180 malate dehydrogenase, 172 pancreatic trypsin inhibitor, 141-142 pipsyl fluoride inhibition of elastase,

92-93 rubredoxin, 359 samarium, 376 tobacco mosaic virus, 436-442 tomato bushy stunt virus, 496 triose phosphate isomerase, 151

a-helix, 589

3t0 helix, 382-383 a-helical coiled-coil, 205-207

Heine crevice in cytochrome c, 400- 401

Heme group in cytochrome b~ structure, 390-394 in cytochrome c, 398-399 in hemoglobin, 295

Heme ligands in cytochrome b~, 390 in cytochrome c, 397

Hemerythrin, 60

Hemocyanin, 60 Hemoglobin, 295-323, 325-341, 343-

357, 546-549 BME-deoxy, structure of, 300 Bohr effect and effect of 2,3-DPG,

3O2-303 a chain salt bridge removal, 312-

313 /~ chain salt bridge removal, 311-312 constrained and relaxed forms,

structure of, 295-296 constraints in the deoxy form, 300-

3O2 constraints, release of ligand bind-

ing, 301-302 cooperative effects, stereochemical

interpretation, 295-310 effect of removal of C-terminal

residues, 311-314 trigger, 296-300

cooperativity, models for, 331-335 crystallization effect on molecular

structure of, 308-309 dissociation of deoxy des- (Arg

141a), 313-314 DPG binding of trifluoroacctony-

lated, 547-548 evolution, 352-353 Glycera hemoglobin

function, 356 strnctnre of, 350-352

hybrid hemoglobins, 325 structure of, 329-330

iron, out of heine plane displace- ment of, 299

kinetics of oxygen binding, 337 lamprey hemoglobin

function, 353-356 structure of, 349-357

mutant human hemoglobins, structure of, 315-323

order of reaction of subunits, 308 oxy- and deoxy- structures at low

resolution, 396 oxygen binding to trifluoroacctony-

lated, 546-547 partially liganded ferrous hemo-

globin, structures of, 330-331 spin-label binding site, 329

Hemoglobin (continued)

t ritluoroacetonylated methemoglobin, 548-549

Hemoglobins Kansas and Richmond, structure of, 318-319

Hemoglobin Rainier relation of structure to abnormal

function, 317-318 structure of, 316-318

Hemoglobin M Iwate comparison with BME-hemoglobin,

320-32 l deoxy vs. methemoglobin compari-

son, 319-320 relation to quaternary structure

change and heine-heine interaction, 321-322

Hexokinase, 166, 592 High-potential iron-sulfur protein,

381-395 Histidinyl residues

NMR of in S. nuclease, 251 Human wart virus, 490

Icosahedral symmetry, 483-486, 489 of satellite tobacco necrosis virus,

483-488 of tomato bushy stunt virus, 491-

493, 495 Imidazole, 8 Immunoglobulins, 413-425, 427-432

human myeloma, 421-425 Indolacyloyl-chymotrypsin, 78-80 Induced fit, 66 Information transfer, 57 Inhibitor complexes with enzymes in

crystals, 143, 248, 249 carbonic anhydrase, 227-229 earboxypeptidase A, 563-565 chymotrypsin, 63-65, 86-88 complexes with proteinases, 148-149 elastase, 98-100 lactate dehydrogenase, 183-186 ribonuclease-S, 39-42 staphyloccal nuclease, 248-249 trypsin, 125-131 trypsin-inhibitor complexes with

trypsin, 137-139

Insulin, 233-241 difference between two molecules

related by non-crystallographic two-fold axis, 233, 236-239

structure of, 233-239 structure and sequence relation to

activity of, 239-241 Intercalation, 263-270 Ion binding sites: thallium, potassium,

sodium sites in subtilisin, 109

636 SUBJECT INDEX

Iron, 53-62 in hemeproteins, 54-58

cytochrome bs, 390 cytochrome c, 398-399 hemoglobin, 295, 299

in non-hemeproteins, 58-61 high potential iron protein, 382-

385 rnbredoxin, 366

Iron-sulfur cluster, 381 structure of, 383-385

Isomorphous replacement method as applied to fibers, 433

Isotope studies of mechanism, 157-164

K

a-Ketoglutarate dehydrogenase complex, 199--203

Kinetic analysis of protein conformation changes, 193-194

Kinetic order, 25

L

Lactone, 24-25 Lactate dehydrogenase, 183-189

abortive ternary complex, 184--186 apoenzyme structure at 2.5 A resolu-

tion, 179-183 binary complex with coenzyme and

coenzyme inhibitors, 183-184 conformation change on binding

NAD § and pyruvate, 186 fit of sequenced peptides to apo-

enzyme map, 183 interaction with NAD + in binary

complex, 188 interaction with NAD + in ternary

complex, 189 peptides around active site, 186-188 substrate interactions, 189 X-ray diffraction studies, 179-191

Lamprey hemoglobin, 349-357 Lectin, 277 Lipase, 5

Lipoyl transsuccinylase, 199-203 electron microscopy of crystals, 199-

200 X-ray diffraction studies, 200-203

Lysozyme, 47, 541-544 complex with trifluoroace~.ylated

analog of chitotriose, 541-544 mechanism, role of distortion in, 29-

33 transition state analogs of substrate

for, 47

M

Magnetic circular dichroisnr, 520 Magnetic resonance methods, 533-540 Malate dehydrogenase, 171-178

crystallization, 172 dimer, 172 heavy atom derivatives, 172 local symmetry of dimer, 174 low resolution electron-density

maps, 173-174 NAD § binding to crystals, 174-175 X-ray diffraction studies of, 171-178

Membrane-bound protein, 387 Metalloenzyme, 561 Method of Bragg ellipses, 437~t39 Methyl (His 57)-ct-chymotrypsin, 67-

69

Michaelis complex, 65-66

Model-building into electron density, 580-581

Model reactions, 21-27

Multi-enzyme complex structural studies, 199-203

Muscle, 277 actin, tropomyosin and troponin in,

214-216 Mutant human hemoglobins, see

Hemoglobin Myeloma lgG, 421 Myogen, 217-220 Myoglobin, 343-348

C.P.K. model of, 585 neutron diffraction studies, 569-575 and hemoglobin, 54-58

N

NAD § 172 Negative cooperativity, 175-178

in alkaline phosphatase, 177-178 Neutron cross-sections, 569 Neutron diffraction, 590 Neutron diffraction analysis of myo-

globin, 569-575 Nuclear magnetic resonance (NMR),

561,590 hemoglobin studies with, 337-341 lysozyme mechanism studies, 29-33 spectrum interpretation using model

building program, 582-583 studies of denaturation of S. nu-

clease, 257-261 studies on elastase, 95-96

Nuclease, 243-256 Nuclease-T, 243

recombination of fragments of S. nuclease to give active enzyme, 253, 254

O

Optically active chromophores and enzyme conformation, 521-524

Orbital steering, 21-22 CNDO/2, 23 con, 21-27 covalent bonds, 22 force constants, 22 lactonization, 23 non-bonded repulsions, 23-24 orbitals, 22-23 pro, 13-20 vibrational amplitudes, 23

Orientation factors in enzymatic catalysis, 13-21, 24-25, 66

effect of slight changes in orientation, 18-19

experimental, 17-19 theoretical, 14-17

Oxygen-uptake, 56

P

Pancreatic trypsin inhibitor, 141-150 homologous inhibitor from bovine

colostrum, 146 model for binding to trypsin, 137-

138 model of inhibitor-proteinase com-

plex, 147-148 reactive site, 146 structure of, 142-146 X-ray diffraction studies of, 141-

150 Papain, 2-3 Paramagnetic probes, 533 Perturbed angular correlations of

gamma radiation, use for study of macromolecules, 511-515

Perturbed angular correlation studies, ribonuclease, 513-514

Phosphofructokinase, 166 Phosphoglucomutase, 61, 160 Phosphoryl-transferring enzymes, 533-

540 Phosphoglncose isomerase, 166 Phosphoglycerate kinase, 167-168 Phosphoglycerate mutase, 169

Phosphorylase, 160 Pipsyl-fluoride, inhibition of elastase,

92-93 /~-Pleated sheets, 589 Polymorphism, 213-214 Pre-transition state proton transfer, 10,

66-67 Propinquity, 24 Prosthetic group-apoprotein inter-

action in hemoglobin and myoglobin, 343-348

SUBJECT INDEX 637

Protein 19F-NMR spectroscopy, 541- 549

Protein-nucleic acid interactions, 35- 43

Protein-nucleic acid recognition, 268- 269

Protein strain, 53-61, 66 Protein structure, distribution of polar

and non-polar residues in, 35-43, 245-248

Proton magnetic relaxation, 551-558 Proton relaxation, 564 Proton relaxation theory, 552-553

Mn ++ ago-ion, 552-553 Mn-carboxypeptidase, 553

Proton transfer, 66, 162-163 Proximity, 21-27, 66

effect, 13-14 Pulsed NMR studies, 405-411 Pyruvate kinase, 169-170, 533-536

R

Rate enhancement, entropy factor, 25- 26

Refinement, 590 of rubredoxin structure, 361-366

Regulation of muscle contraction, 215- 216

Regulatory enzyme, 193-198, 285-290 Relaxation studies, 193-198 Repressor and operator symmetry,

268 Respiratory chain, mitochondrial, 397 Restriction, 268-269 Ribityl phosphate, 373 Ribonuclease

denaturation, 513 perturbed angular correlation stud-

ies, 513-514 reduction, partial, 513 transition state analogs of substrates

for, 48-50 Ribonuclease-S, 35-43

conformational changes in, 544-546 "in line" mechanism, 40-42 interactions of S-peptide and S-pro-

tein, 37-39 nucleotide binding to, 39-42 X-ray studies of, 35-43

Rotation function application to satellite tobacco ne-

crosis virus for determination of particle symmetry, 471-473, 483- 486

tomato bushy stunt virus, use on, 496

Rotational tracers, 511 111cadmium, 511 ltaindium, 511 in mice, 514-515

Rubredoxin, 60, 359-367 iron-ligand structure, 366 refinement by AF synthesis, 364

by full matrix least squares, 365- 366

of structure, 361-366

Satellite tobacco necrosis virus, 469- 488

number of protein subtmits in shell of, 469-470

rotation function use to determine particle symmetry, 471473, 483- 486

symmetry and orientation of particle, 471-473

symmetry of protein shell icosahedral, evidence for, 483-488 octahedral, evidence for, 471-482

Screenless precession photography, 381 Semicarbazones, 7-8 Sequence determination of calcium-

binding protein, 218-219 Serine proteases, comparison of speci-

ficity sites, 131-132 Solvation, 24-25 Solvent accessibility in protein struc-

ture, 35-37 changes occurring on association of

UpcA with RNase-S, 42 main chain, 36-37 non-polar groups, 35-36 polar groups, 35-36

Solvent perturbation, staphylococcal nuclease, 250

Space-filling models of proteins, 585- 586

Specificity, 66 Spectro-chemical probes, 517-531 Spectrophotometric studies of protease

catalysis, 75-83 Spherical virus structure, 469-501 Spin label, 325-336 Spin-labeled triphosphate, 325-336 Spin-state change, 54 Staphylococcus aureus extracellular

nuclease, 243-256 Staphylococcal nuclease, 257-261

distribution of polar and non-polar residues in structure, 245-248

inhibitor binding site, 248, 249 mechanism, 248, 249

Steric compression, 21 Steric hindrance, 54 Strain, 21

enzyme, 53-62, 66 relief vs. orientation, 17-18 substrate, 29-33, 45-51, 66

Streptomyces griseus trypsin, 133 structural homologies, 126-139

Structnre-reactivity correlations, 1-10 Substrate binding sites, comparison of

elastase and chymotrypsin, 99- 101

Suhstrate complexes, lactate dehydrogenase, 189

Subtilisin, 107-123 comparison of BPN' and Novo, 107-

116 peptide chloromethyl ketone deriva-

tive, 117-120 resemblance to chymotrypsin, 121-

123 substrate binding site, 118-123 X-ray diffraction studies of BPN',

117-123 Snbtilisin BPN', 107-116 Subtilisin Novo, X-ray diffraction

studies of, 107-116 Syncatalytic, 517

chemical modification, 517-519 Synchrotron radiation, 590 Synthetic analogs, 251

T

Tomato bushy stunt virus (TBSV), 490-493

chemical composition of, 495 radial distribution of density in,

495-496 RNA arrangement in, 499-500 structure determinatiou by image

reconstruction from electron micrographs, 490-493

three-dimensional model of (X-ray studies), 498-499

X-ray diffractiou analysis at 30 A resolution, 495-501

Tetrahedral intermediate, 6, 66, 79 Tetranitromethane, 517 Tetrazolylazocarbobenzoxytyrosine,

525 Thin filament

functional unit, 215 length regulation, 215

Thiol esters, 3-4 Three-dimensions, computer display

representation of, 578-579 Three-dimensional image reconstruc-

tion, 489-494 Thymidine dephosphate, 243 Tobacco mosaic virus (TMV), 433-448

assembly with disks, 462-465 association of protein into disks,

453-455 control mechanism in the polymeri-

zation, 455-456

638 SUBJECT INDEX

Tobacco mosaic virus (continued) conversion from disks to helix, 457-

458 diffraction from gels of, 433-434 electron-density map at 10 A resolu-

tion, 443-445 helical nature, 433 location of RNA chain ill, 445 mechanism and control of assembly

from RNA and protein disks, 461-468

mode of protein aggregation, 449- 460

phase diagram of TMV protein, 449-451

structure of disk of protein, 451- 453

three-dimensional Fourier from two- dimensional data, 434

titration of protein, 461 Tosyl fluoride, inhibition of elastase,

91 Transition state analogs, 45-51

chymotrypsin, 47-48 lysozyme, 47 ribonuclease, 48-50 triosephosphate isomerase, 152

Triosephosphate dehydrogenase, 167 Triosephosphate isomerase, ]51-155,

157-164, 167 active site, 153-154 changes with phosphate mother

liquor, 154 conformational, changes on substrate

binding, 152 energetics of the catalyzed reaction,

162 heavy atom derivatives of, 151 isotope effect, 161 isotopic discrimination in product

formation, 158-160 low temperature mother liquors for,

154 mechanistic pathway studies, 157-

164

Triosephosphate isomerase (continued)

molecular weight of, 151 pathway, 157-158 proton transfer, 162-163 transition state analog, 152 X-ray diffraction studies of, 151-

155 Troponin, 205, 217

calcium binding to, 215-216

Tropomyosin, 205-216 axial period in muscle, 215 bonding sites in crystal, 212 cooperative transitions in crystals,

215-216 heavy atom derivatives, 209 interaction sites, 211-212 length, 215 molecular packing in crystals, 209-

210 phasing by Bragg method, 209 polymorphism, 212 preparing crystals and recording dif-

fraction pattern, 205-206 sequence, 205 suhunits, 205 symmetry of crystals and cell dimen-

sions, 206-207 tactoids, 213 troponin binding to crystal, 212

Trypsin calcium ion effect, 136-137 conformational changes, 131 homology with chymotrypsin, 131-

135 pancreatic trypsin inhibitor complex

crystallization, 148-149 specificity, structural explanation

for, 131 X-ray diffraction studies of, 125-140 zymogen activation, 135-137

Trypsinogen, 135-137 Turnip crinkle virus, 490, 493 Tyrosyl nitration, 517-518

Tyrosyl residnes, exposure in S. nuclease, 250

U

Unfolding and refolding of S. nuclease, 257-261

V

Virus assembly, 500

W

Water structure, 590

X

X-ray diffraction methods Bijvoet difference Fourier map, 371,

383 computer-controlled display system,

577-583 computer-drawn packing models of

proteins, 35-36 crystallization, using micro-diffusion

cells, 291 densitometry of films, 217

computer-controlled, 436 electron micrographs used to phase

X-ray diffraction patterns, 202- 203

refinement of protein at 1.5 A resolution (by full matrix least squares), 361-366

screenless precession photography, 381

Z

Zero field splitting, 551 Zinc

in carbonic anhydrase, 226-228 in carboxypeptidase A, 561,563 in insulin, 238-239

Zymogen activation, 521-523

N A M E I N D E X

A

Abita, J. P. 136, 137, 147 Abragam, A. 512, 556 Abramowitz, N. 96 Acher, R. 145 Adams, M. J. 174, 179-191,

223,233 Adamson, J. w . 315 Adler, A. 343 Agrawal, B. B. L. 271,283 Ainsworth, C. F. 271-276,

427--432 Akervall, K. 469-488 Akesson, A. 402 Albery, J. 163 Alden, R. A. 107, 117-123,

134, 381-385 Allen, D. W. 353,547 Allen, L. 171, 176 Allewell, N. M. 35-43 Allison, M. J. 369 Allison, W. S. 179, 183, 186,

188, 189, 190 Ames, B. N. 326 Amiconi, G. 344, 345, 347 Amos, L. A. 451, 452, 460,

489-494, 495, 498-500 Amzell, L. M. 421-425 Anderer, F. A. 141 Andersen, M. E. 314, 354,

356 Andersen, R. D. 369-379 Anderson, D. G. 50 Anderson, R. G. 525 Andreyeva, N. S. 167 Anfinsen, C. B. 243, 246, 247,

249-255 Anisowicz, A. 351 Ansevin, A. T. 449, 455 Anson, M. L. 561 Antonini, A. 325,334 Antonini, E. 307, 312, 313,

340, 341,354, 549 Anwar, R. A. 96 Apgar, P. A. 369-379 Arata, Y. 257-261 Arber, W. 269 Argos, P. 387-395 Arison, B. H. 265 Arley, N. 31 Armstrong, J. McD. 221 Arndt, U. W. 436 Arnon, D. 381 Arnone, A. 243,248, 309 Arnott, S. 184 Arquilla, E. R. 241 Asakura, T. 332, 335

Atabekov, J. G. 462 Atassi, M. Z. 253 Atlas, D. 96, 97, 100 Aune, K. C. 85 Avey, H. P. 421-425

B

Bachmayer, H. 359, 360 Bailey, J. E. 303 Bailey, K. 205 Baldassare, J. J. 334 Baldeschwieler, J. D. 511,

515 Baldwin, J. M. 151,304, 322 Ballhausen, C. H. 528 Ballhausen, C. J. 13 Banaszak, L. J. 167, 171-178 Banerjee, R. 57 Banner, D. W. 151-155, 157,

167 Barber, E. D. 197 Barfield, M. 29 Barnard, E. A. 40 Barnett, R. E. 9 Barrett, A. N. 433-448 Barrington Leigh, J. 433-

448 Barry, C. D. 577-584 Bartsch, R. G. 381,385 Basolo, F. 343 Becka, L.-N. 421-425 Becker, J. W. 277-284 Beckert, W. H. 277 Beddell, C. R. 581 Behlke, J. 355 Behme, M. 264 Behnke, W. D. 523 Beinert, H. 377 Bell, J. D. 291-294 Bell, R. P. 161 Bencze, W. L. 480 Bender, M. L. 1, 8, 67, 75,

76, 79, 88, 96 Benedetti, E. 527 Benesch, R. 302, 312, 325,

326, 327, 329, 334, 335, 337, 343

Benesch, R. E. 302, 312, 325, 326, 329, 337,343,547

Bengtsson, U. 221-231 Benkovic, S. J. 8, 21, 24, 25 Benson, S. W. 16 Berger, A. 78, 87, 96, 119 Berger, J. E. 486 Bergst6n, P.-C. 221-231 Bernal, J. D. 433, 589 Bernardi, G. 268 Bernfield, M. K. 37

Bernhard, S. A. 64, 75--83, 107

Bernheim, R. A. 555 Best-Belpomme, M. 198 Bethpage, P. H. 561-567 Beychok, S. 225 Bhargava, N. 141 Bier, C. J. 243-255 Bigelow, C. 514 Biltonen, R. 131 Birk, Y. 91 Birktoft, J. J. 63, 85, 94, 95,

107, 117-123, 125, 134, 137, 189

Birnbaum, E. R. 377 Blake, C. C. F. 29, 47, 543,

581 Bleaney, B. 556 Bloembergen, N. 552 Bloom, B. 157 Bloomer, A. C. 151-155 Blout, E. R. 96, 97, 100 Blow, D. M. 9, 63-70, 85, 95,

100, 113, 114, 116, 117, 122, 125, 147, 151, 174, 180, 186,221,278,286, 288,371, 423, 471, 496, 506, 522

Blumberg, W. E. 56 Blundell, T. L. 233-241 Bolton, W. 295, 308, 311,

319 Bonaventura, J. 306, 315,

316 Booth, V. H. 227 Bradbury, E. M. 96 Bradbury, J. H. 535 Bradbury, S. L. 229, 566 Bradbury, W. M. 21,24, 26 Bradshaw, R. A. 129, 172,

217-220, 556 Br/ind4n, C.-I. 363, 503-510 Bragg, W. L. 209, 309, 436,

591,592 Brandenburg, D. 241 Breiger, H. 171 Bridgeman, P. W. 519 Briehl, R. W. 302, 313, 329,

354 Bright, H. J. 197 Brill, A. S. 238 Britten, H. T. S. 49 Brouwer, D. M. 3 Brown, H. 233 Brown, J. E. 37 Brown, R. D. 551-559, 561-

567 Brown, W. 214, 215,216 Bruice, T. C. 3, 4, 8, 14, 16,

21-27, 78 Brundell, J. 221 Brunori, E. 549

639

Brunori, M. 295, 325, 341, 347

Bryan, R. F. 217 Bucci, E. 337 Buehner, M. 179-191 Bunn, H. F. 302, 313, 329 Bunnett , J. F. 21 Burger, M. M. 271,277 Burton, P. M. 162 Butler, P. J. G. 455, 456,

457, 459, 461--468, 480, 482, 491, 492, 493, 495, 500

Burnett, R. M. 369-379 Busing, W. R. 272, 371,424 Butt, W. D. 402 Bywater, R. P. 293

C

Campbell, J. w . 165-170 Cantor, C. R. 325, 526 Caplow, M. 5, 6, 7, 8, 66, 67 Carlbom, U. 221-231 Carlson, W. D. 35-43 Carpenter, F. H. 241 Carpenter, J. M. 456 Carraway, K. W. 13-20 Carrell, R. W. 315 Carter, C. W., Jr. 381-385 Caspar, D. L. D. 201, 203,

205-216, 433, 438,449, 454, 455, 457, 459, 461,462, 469, 486, 489, 491,494, 496, 499, 500, 503, 504, 509

Cassoly, R. 330, 332, 337, 338 Cechova, D. 146 Cerami, A. 263, 264 Chadwick, P. 268 Chaiken, I. M. 243, 246, 247,

251,254 Chance, B. 107,356 Changeux, J.-P. 295,332 Chanutin, A. 329, 332 Charache, S. 315, 319 Charles, M. 129 Charney, E. 77, 78 Chasteen, N. D. 48 Chauvet, J. 141,145 Chiancone, E. 341 Chiang, J. F. 17 Chipman, D. M. 29 Chow, R. B. 145 Christen, P. 517 Christian, W. 168 Cochran, W. 433, 569 Coffee, C. J. 217-220 Coggins, J. R. 575,585-587 Cohen, C. 205-216 Cohen, G. H. 85-90, 107

640 N A M E I N D E X

Cohen, G. N. 194, 195, 196, 198

Cohen, L. A. 21,517, 519 Cohn, M. 533-540, 553,558 Coleman, J. E. 229, 551,554,

564 Commoner, B. 449 Connick, R. E. 533 Conti, F. 265 Coon, M. J. 359 Cope, A. 18 Cordes, E. H. 264 Corey, R. B. 85, 375, 508,

589 Cornforth, J. w . 179 Cornick, G. 505, 509 Coryell, C. D. 298 Cotton, F. A. 243-255 Coulson, A. F. W. 157, 161 Cox, J. M. 151 Crane, H. R. 467 Crick, F. H. C. 151, 180, 205,

221,278, 288,371,423,433, 442, 473, 497,592

Crothers, D. M. 263, 264 Crowther, R. A. 200, 430,

432, 451, 452, 482, 489- 494, 495, 498, 499, 500

Crumbliss, A. L. 343 Crumpton, M. J. 253 Cuatrecasas, P. 247, 249, 250 Cullis, A. F. 174, 371 Cunningham, B. A. 283, 284 Cunningham, L. W. 88 Curnish, R. R. 329 Cusumano, C. L. 243 Cutfield, J. F. 233-241

D

Dafforn, G. A. 13-20 Dahlquist, F. W. 29, 353,

543,544 Dale, B. W. 56 Danchin, A. 553, 558 Dangelat, D. 217 Danyluk, S. S. 265 Darnall, D. W. 377 Dastoor, M. N. 291-294 Davies, D. R. 64, 67, 125,

413--419 Davies, R. C. 523 Davis, R. P. 299 Day, L. 508 Day, V. W. 243-255 Dayhoff, O. M. 129, 316,

352, 478 De Graaf, M. J. M. 107 De Klerk, H. 381 Delaage, M. 131 del Putsinelli, P. 295 del Rosario, E. J. 50 Dennaro, A. E. 227 DeRosier, D. J. 199-203,

454, 489 De Santis, P. 265 Deutsch, H. F. 427,432 Devenyi, T. 171 De Vijlder, J. J. M. 193 Diamond, R. 142, 233, 578 Dickerson, R. E. 125-140,

219, 272, 287,352, 359, 371, 375, 377,393,397--404, 407, 409, 410, 411, 428, 440

Dixon, M. 50, 161 Dlouha, V. 141 Dodson, E. J. 233-241 Dodson, G. G. 233-241 Dolphin, D. 29-33, 47 Donohue, J. 265 Doonan, S. 67 Douzou, P. 155 Dowsing, R. D. 556 Doyle, R. J. 275 Drabikowski, W. 217 Draper, R. D. 369 Drenth, J. 95, 107-116, 223 Dreyer, W. J. 71 Drott, H. R. 332, 335 Dubin, D. T. 326 Dubourdieu, M. 369 Dude, F. 165-170 Dugas, H. 93, 96 Dunn, M. 83 Durham, A. C. H. 294, 449-

460, 461,462, 463,465 Dus, K. 381, 382

E

Eagles, P. A. M. 166 Eaker, D. 469-488 Eaton, W. A. 59 Ebashi, F. 215 Ebashi, S. 205, 214, 215, 216,

217 Eberson, L. 21 Eck, R. V. 352 Eckstein, F. 42 Edelman, G. M. 280, 282,

283, 284, 416, 417 Edelstein, S. J. 295, 306, 319,

334, 340 Edmondson, D. E. 369, 375,

377, 378 Edmundson, A. B. 271-276,

427--432 Edsall, J. T. 221, 229, 573,

585 Edwards, B. F. P. 285-290 Efremov, G. D. 315,316 Ehrenberg, A. 227,377 Eigen, M. 163, 194, 198 Eisenberg, D. 291-294 Eliel, E. L. 29 Elkins-Kaufman, E. 563,

564 Ely, K. R. 427-432 Endo, M. 205,215 Englard, S. 171 Epand, R. M. 67,253 Epstein, H. F. 251,253 Ericksson-Quensel, I. B. 350,

354 Esnouf, P. 157 Evans, D. R. 285 Evans, M. C. W. 381,384

F

Fabry, M. E. 229, 411,566 Fabry, T. L. 548 Fairclough, G. F. 522 Falkmer, S. 239, 240 Fankuchen, I. 433

Felton, S. M. 4 Ferdinand, W. 172 Ferentz, H. 512 Fernando, q. 48 Fersht, A. R. 3, 10, 71-73 Finch, J. T. 287, 436, 449,

451,452,454, 456,463,466, 482, 486, 489, 490, 491,492, 495, 498, 500, 503

Finkenstadt, W. R. 146 Fish, W. W. 478 Folk, J. E. 311 Fondy, T. P. 179 Ford, G. C. 179-191 Forsen, S. 405 Foster, J. F. 478 Foster, M. E. 60 Foust, G. P. 369 Fox, J. L. 378 Fraenkel-Conrat, H. 455,

459, 461,462 Franklin, R. E. 433,435,

436, 439, 443,449, 486 Franklin, R. M. 503-510 Franks, W. A. 285-290 Freer, S. T. 67, 71, 107, 122,

125, 134, 136, 137, 381-385, 522

Fridborg, K. 221-231, 469- 488

Frieden, C. 193, 198 Fritz, H. 137, 145, 147 Fronticelli, C. 337 Fuchs, S. 250, 254 Furth, A. J. 151

G

Gaber, B. P. 556, 558 Garby, L. 329, 332 Gass, J. D. 13-20 Gates, V. 29, 107 Gawron, O. 5 Geis, I. 219 Gellert, M. 264, 268 Geneste, P. 96 George, P. 547,548 Geraci, G. 312, 337 Gerding, R. 171 Gergely, J. 205,217 Gerhart, J. c. 285 Gerstein, J. 3 Gertler, A. 91, 96, 97 Ghelis, C. 131 Gibson, Q. H. 193, 308, 313,

339, 340, 354, 356 Gilbert, P. F. C. 448, 449,

452, 454, 462 Gilbert, W. 268 Gilchrist, M. 3, 82 Gillespie, R. J. 23 Ginsberg, H. S. 503 Glatthaar, B. E. 172, 175,

176 Goldberg, I. H. 263,264,

268 Goldstein, D. J. 417, 421-

425 Goldstein, I. J. 271,277, 283 Goodkin, P. 291-294 Goodman, M. 253,527 Goryunov, A. I. 166, 167 Gossling, T. H. 580 Gdthe, P. O. 229

Graham, D. 221 Gray, R. D. 307 Greaser, M. L. 205,217 Green, D. W. 433 Green, M. 575 Green, N. M. 137, 141, 146,

147, 417 Greene, L. J. 146, 147 Greenzaid, P. 5 Greer, J. 272, 273, 277, 295,

306, 311,315-323 Gregory, J. 433 Griffith, J. S. 556 Grisola, S. 168 Grogan, R. G. 469 Gueron, M. 553,558 Guerritore, D. 349 Guidotti, G. 312, 313 Gundlach, H. G. 40 Gupta, R. K. 397, 399, 402,

405-411, 552, 558, 566 Gurd, F. R. N. 107 Gustafsson, L. 477 Gutfreund, H. 177, 179, 190

H

Haas, D. J. 186 Haber, E. 218 Hackert, M. L. 171-191 Halford, S. E. 177 Hall, P. L. 566 Hamilton, C. L. 511 Hamilton, H. B. 305, 312 Hamilton, L. 263 Hamilton, W. C. 345 Hammes, G. G. 50, 162, 194 Hammond, G. S. 46 Hamoir, G. 217 Hanania, G. 547,548 Hanshoff, G. 285 Harbury, H. A. 377 Hardman, J. K. 461 Hardman, K. D. 271-276,

427-432 Hardy, R. W. F. 369, 377 Hargrave, P. A. 169 Harker, D. 434 Harrison, S. C. 206, 493,

495-501, 503-510 Hart, R. G. 151 Hartley, B. S. 91, 94, 125,

129, 133, 218 Hartman, F. C. 157,161 Hartshorne, D. J. 205 Hartsuck, J. A. 561 Haschemeyer, A. E. V. 184 Haselkorn, R. 264 Hauschka, P.V. 585 Hauser, C. F. 21 Hausser, R. 552 Hayashi, A. 315,316 Hayashi, N. 315 Hazen, E. E., Jr. 243-255 Hearn, R. P. 39 Heck, H. d'A. 179, 197 Heidema, J. H. 148 Heidner, E. G. 291-294 Heins, J. N. 249 Heller, P. 316, 322 Henderson, L. 221, 223, 225,

229 Henderson, R. 63-70, 78, 96,

100, 101, 117, 148

N A M E I N D E X 641

Hendrickson, W. A. 299, 349-357

Henry, N. F. M. 274 Herd, A. K. 21 Hermann, E. 329, 332 Hermans, J., Jr. 513 Herries, D. G. 49 Herriott, J. R. 359-367, 383 Hess, G. P. 63-70, 71 Heuhns, E. R. 308 Hewitt, J. A. 303, 305, 307,

308, 311-314 Higashi, S. 212 Higashi-Fujime, S. 211, 212,

213 Higuchi, T. 21 Hill, E. 171-178 Hill, H. O. A. 54, 56, 59 Hinkle, P. M. 76, 77, 82 Hitchcock, S. E. 214, 216 Hjertfins, S. 469-488 Ho, C. 334 Hoard, D. E. 325 Hoard, J. L. 299, 347, 355,

356, 549 Hochstrasser, K. 147 Hochstrasser, R. M. 59 Hodges, R. S. 205 Hodgkin, D. C. 233-241, 349 Hodgson, G. 165-170 Hofmann, R. 13 Hofmann, T. 96, 97 Hoffman, B. M. 299, 343-

348 Hoffmann, R. A. 405 H6glund, S. 430, 469, 476,

481, 503 Hol, W. G.J. 107-116 Holasek, A. 430 Holbrook, J. J. 179 Hollenberg, P. F. 169 Holmes, K. C. 205, 287, 433-

448, 454, 462 Holtzer, A. 205 Hoogsteen, K. 265 Hopfield, J. J. 337-341 Horecker, B. L. 402 Home, R. W. 503 H6rnle, S. 141 Horowitz, M. S. 504 Howell, S. F. 271,277,283 Hoyle, N. J. 56 Hubbard, C. D. 7 Huber, R. 64, 100, 134, 139,

141-150, 299, 349, 351, 352 Huestis, W. H. 541-550 Huggins, M. L. 223 Hugli, T. E. 107 Hukins, D. W. L. 184 Hultquist, D. E. 387 Humphrey, R. L. 421--425,

427 Huntley, T. E. 387, 393 Hurwitz, J. 263 Huxley, H. E. 214, 215,216

Ibers, J. A. 344, 345,347 Igelstr6m, M. 2 Imai, K. 311,312 Inagami, T. 5, 6, 66 Inbar, M. 271,277 Ingles, D. W. 64

Ingold, C. K. 24 Ingraham, L. L. 369 Inward, P. W. 4, 66 Irving, H. 54 Ivanov, V. I. 518 Iwatsubo, M. 195, 196, 197,

198

J

Jacob, F. 193 Jacobus, J. 188 Jain, S. C. 263-270 Janin, J. 193-198 Jansonius, J. N. 107-116 Jardetzky, O. 250, 257-261,

545 Jfirup; L. 221-231, 470 Jeckel, D. 179, 188 Jencks, W. P. 1-11, 21, 24,

25, 26, 46, 47, 66, 82, 163, 346, 591

Jensen, L. H. 359-367 Johannisen, H. 469-488 Johansen, J. T. 517-531 Johnson, C. D. 172 Johnson, C. H. 67 Johnson, L. N. 29, 151, 152,

153, 154, 157 Johnston, H. S. 23 Jones, R. T. 306, 316 Jonxis, J. H. P. 402 Josephs, R. 507

K

Kfiji, J. H. R. 402 Kalb, A. J. 271,274, 277 Kallai, O. B. 397-464 Kallos, J. 107 Kamen, M. D. 381 Kandel, M. 229 Kannan, K. K. 171, 221-231,

469-488 Kaper, J. M. 500 Kaplan, H. 93, 96 Kaplan, N. O. 171,188, 190 Karpeisky, M. Y. 518 Karplus, M. 29 Kartha, G. 107,513 Kassanis, B. 469, 480, 481,

483 Kassell, B. 141,145 Katz, J. J. 541 Katze, J. R. 157 Kauzmann, W. 449 Kay, C. M. 275, 280 Kay, L. M. 125-140 Kayne, F. J. 169, 534, 535 Keil, B. 478 Keilin, D. 227, 402 Keizer, J. 78 Kellett, G. L. 308, 313 Kelly, T. J. 268,269 Kendrew, J. c. 349, 440,577 Kennel, S. J. 381 Kernohan, J. C. 566 Kersten, W. 263, 264 Keyes, M. H. 344, 345 K~zdy, F. J. 1, 78, 79 Khalifah, R. G. 229

Khan, M. M. T. 49 Kierkegaard, P. 378 Kilmartin, J. V. 303, 305, 307,

308, 311-314, 315, 321, 547 King, N. L. R. 535 Kirk, J. 263 Kirsch, J. F. 2, 7, 8, 76, 77,

82, 83 Kirschner, D. A. 209 Kirschner, K. 193 Kishida, T. 129 Klee, W. A. 37 Klock, P. A. 349-357 Klug, A. 199, 200, 433-448,

449-460, 461-466, 469, 471, 480, 482, 483-488, 489-491, 494, 495, 500, 503, 504

Knappe, J. 369 Knight, C. A. 465, 500 Knight, E., Jr. 369, 377 Knopf, P. M. 432 Knowles, J. R. 64, 67, 157-

164 Kodama, A. 215 Koehler, K. A. 45-51, 82 Koekoek, R. 107-116, 179 Koenig, S. H. 551-559, 561-

567 Koenigsberg, W. 312 K6nig, E. 54 Konosu, S. 217 Kornberg, A. 402 Koshland, D. E., Jr. 13-20,

21-23, 25, 193, 331, 332, 337, 518, 541

Kosower, E. 75 Krahn, J. 145 Kratky, O. 477 Kraut, H. 141 Kraut, J. 95, 117-123, 273,

371,381-385, 388 Kress, L. F. 64, 143,145, 146 Kretsinger, R. H. 217-220,

288, 387 Krumholz, P. 54 Kukla, D. 141-150 Kunitz, M. 141 Kuntz, I. D. 496 Kurooka, S. 166

L

Labaw, L. W. 413-419, 482 Laidler, K. J. 45 Lapinski, R. 3 Lardy, H. 171 Larsen, S. 243-255 Larson, J. 263, 264, 265, 266,

267 Laskowski, M. 64, 138, 141,

143,145, 146, 147,148 Latt, S. A. 61, 519, 520, 527,

529, 535 Lattman, E. E. 349-357 Lau, S.-J. 75-83 Laurent, G. 221,229 Lauffer, M. A. 449, 454,455 Laukien, G. 552 Laver, W. G. 503, 504, 505,

5O7 Lazdunski, M. 131, 137 Leach, S. 170 Leadlay, P. F. 157-164

Leberman, R. 184, 433--448, 486, 492, 495

Lederer, C. M. 511 Lee, B. 35--43, 245,248 Le Gall, J. 369 Legge, J. w . 349, 355 Lehmann, H. 315, 319 Lehn, J. M. 115 Leigh, J. S., Jr. 533-540 Leipert, T. K. 511 Lemberg, R. 349, 355 Lentz, P. J., Jr. 179-191 Leon, M. A. 271,277 LeQuesne, M. E. 369-379 Lerman, L. S. 263 Lesnaw, J. A. 470 Levine, M. 387-395 Levinthal, C. 578, 579 Levitski, A. 271,277 Levitt, M. 233 Levy, H. A. 371,424 Levy, M. R. 179 Lewis, H. J. 96 Li, S. L. 349, 355,356 Lieflfinder, M. 221 Liener, I. E. 129, 271,283 Lienhard, G. E. 45-51, 82 Liljas, A. 221-231, 470, 477 Linderstrom-Lang, K. 518 Lindquist, R. N. 45-51 Lindqvist, I. 504 Lindskog, S. 61,223,225,

227,229, 521 Lindstrom, T. R. 56 Linn, S. 269 Lipscomb, W. N. 61, 223,

280, 285-290, 370, 371,375, 524, 526, 556, 558, 561-567

Livingston, D. M. 517-531 Lloyd, K. O. 271 Lo, H. H. 329 Longley, W. 213, 214, 215 Lode, E. T. 359 Lonsdale, K. 274 Love, W. E. 299, 349-357 Lovenberg, W. 359, 381 L6vgren, S. 221-231, 469-

488 Lowe, G. 6, 8, 29 Lowey, S. 211 Lucas, R. M. 205-216, 500 Ludwig, M. L. 369-379 Lumbry, R. L. 407 Lundin, J. 469, 480 Lustig, A. 271,274, 277 Luz, Z. 533 Luzzati, V. 581 Lynden-Bell, R. M. 512, 515

M

Maeda, T. 329 Magdoff, B. 497 Maister, S. G. 157-164 Maizel, J. V., Jr. 503, 504,

507 Malhotra, O. P. 5, 76 Mallett, J. F. W. 436 Malrieu, J. P. 378 Mandelkow, E. 433--448 Mangum, C. 356 Mann, T. 227 Maren, T. H. 221 Margoliash, E. 402, 411

642 NAME INDEX

Markland, F. S. 115, 118 Markley, J. L. 250, 257-261 Marshall, A. G. 512 Martell, A. E. 49, 54 Massey, V. 369, 370, 377 Mathews, F. S. 166, 176, 186,

309,387-395 Matthews, B. W. 63, 80, 85,

87, 91, 107, 148, 149, 218, 292,371,382, 388, 429

Matsubara, H. 115 May, D. S. 465 Mayhew, S. G. 369-379 Mazzarella, L. 335 McConnell, H. M. 325-336,

511,537,582 McCormick, D. B. 377 McDonald, C. C. 410, 535 McFarland, B. G. 325, 537 McGarvey, B. R. 556 McLachlan, A. D. 88 McLaughlin, P. J. 461 McMurray, C. H. 285-290 McPherson, A., Jr. 179-191 McVittie, J. D. 157 Meadows, D. H. 258, 545 Meany, J. E. 221 Meares, C. F. 511-516 Medzyhirasky, K. 96 Meighen, E. A. 285 Melchers, F. 432, 448 Meldrum, N. U. 221 Mella, K. 179, 187, 190 Meloun, B. 145 Mercer, W. D. 165-1q0 Mercola, D. A. 233-241 Meselson, M. 269 Meyer, E. F., Jr. 579, 586 Michelin-Lausardt, P. 480,

482 Mildvan, A. S. 377,533,536 Millar, D. B.S. 179, 188 Millett, F. 541-550 Millward, G. R. 213,215 Milstein, S. 21 Mitsui, Y. 35-43 Mitz, M. A. 563, 564 Monod, J. 193,266, 273,295,

303,307,311,319, 331-333, 337,541

Moore, P. B. 199 Moore, S. 40, 479 Morallee, K. G. 377 Morgan, L. O. 552 Morihara, K. 90, 118, 120,

121 Morimoto, H. 307,319 Moring, I. 469-488 Mueller, M. H. 272 Muirhead, H. 165-170, 295,

296, 311,316, 318-320, 349, 354, 423,424, 429

Mfiller, W. 263,264 Miiller-Hill, B. 268 Mulliken, R. S. 13

N

Nagel, R. L. 315 Najjar, V. A. 166 Nakagawa, Y. 67 Narita, K. 455, 461

Navon, G. 551,553,554, 555, 558, 564

Neet, K. E. 22, 518 Neil, G. L. 87 Nelson, N. 369 Nemethy, G. 223,247 Neumann, J. 369 Neurath, H. J. 71, 88, 521,

522, 563, 564, 565 Nickless, G. 525 Nisonoff, A. 421,425 Nixon, H. L. 480, 481,483 Nobrego, F. G. 391,395 Nockolds, C. F. 217-220 Noda, L. 538 Noelken, M. E. 417 Noller, H. 77 Noltmann, E. A. 163 Nonomura, Y. 214 Noonan, K. D. 271,277 Nordman, C. E. 263-270,

378 Norrestam, R. 378 North, A. C. T. 151, 218,

241,277, 359, 370, 371,382, 577-584

Northrop, J. H. 141 Novoa, W. B. 179 Novy, M. J. 306 Nozaki, M. 402 Nozaki, Y. 514 Nuckolds, C. E. 288 Nyholm, R. S. 383 Nyman, P. O. 221, 225, 229,

521

O

Oakenfull, D. G. 4 Oberg, B. 469-488 O'Connell, E. L. 153 Offord, R. E. 151 Ogata, R. T. 325-336 Ogawa, S. 307, 325, 330, 332,

333, 334, 335, 337-341 Ogunmula, G. 356 Ohnishi, S. 329 Ohtsuki, I. 214, 216 Oka, T. 118, 120 Okazaki, T. 349 Olaitan, S. A. 107 Oliver, R. M. 199-203 Olsen, M. O.J . 129, 134, 271,

272 Olson, J. 8. 308, 339 Olson, M. O. 283 Omenn, G. S. 246, 250, 254 Onda, H. 465 O'Neill, J. J. 3 Ontjes, D. A. 246 Ooi, T. 211,212, 213 Oppenheimer, H. L. 69 Ortony, A. 579 Osborn, M. 206, 479 Oshino, N. 387 Ost, A. 477 O'Sullivan, W. J. 536, 538 o t t , D. G. 325 Ottesen, M. 521,522 Oxelfelt, P. 477 Ozols, J. 387, 390, 391, 393,

395

P

Padlan, E. A. 349-357 Paetkau, V. 171 Page, M. I. 3, 21, 24, 26 Page, S. G. 214 Palmer, G. 370, 377,409, 410 Pandit, U. K. 21, 24, 25 Pardee, A. B. 285 Parikh, I. 254 Parker, C. J. 209 Parker, L. 5, 9, 66 Parkhurst, L. J. 313 Parmeggiani, A. 166 Parravano, C. 31 Parry, D. A. D. 205-216 Parsons, S. M. 544 Passon, P. G. 387 Pasteur, L. 592 Patt, S. L. 29-33 Paul, C. 422 Pauling, L. 13, 45, 47, 78,

222, 298,375, 384, 508, 589, 591

Peacocke, A. R. 552, 558 Pechere, J. F. 217,219, 220 Pedersen, D. M. 478 Peel, J. L. 369 Peisach, J. 56 Penny, I. F. 166 Pereira, H. G. 503-505 Perrin, D. D. 549 Perry, S. V. 205 Perutz, M. F. 54-57, 295--

310, 311-317, 319-322, 325, 329, 334, 335, 340, 347, 349, 351, 354, 355, 546-549, 589

Petef, G. 469--488 Petef, M. 221-231 Petering, D. H. 299, 343-348 Petsko, G. A. 151-155 Pettersson, U. 503-510 Pfleiderer, G. 179, 187, 188,

190 Pflumm, M. N. 280, 283, 284 Philip, G. 5 Philipson, L. 503-510 Phillips, D. C. 29, 151-155,

218, 583,589-592 Phillips, W. D. 381, 384, 535 Pickl, E. 239 Piette, L. H. 360 Pilz, I. 417 Piper, P. W. 96 Pirrotta, V. 268 Plaut, B. 163 Plummer, T. H. 551,558,

566 Pocker, Y. 221 Pogson, C. I. 151-155 Poland, D. 253 Polgar, L. 67 Poljak, R. J. 421-425, 427 polya, J. B. 221 Ponticello, G. 263-270 Pound, R. V. 512 Powell, A. E. 271,277 Powers, J. C. 85-90, 117-123 Prage, L. 503,507 Priddle, J. D. 151 Pringle, J. R. 166 Priyadarshini, U. 49 Ptashne, M. 268 Pullman, B. 378 Putter, I. 257, 541 Piitter, J. 146, 147

Q

Quiocho, F. A. 93, 107, 277- 284, 524, 526, 557, 558, 561-567

R

Rae, A. D. 371 Raftery, M. A. 541-550 Ramachandran, G. N. 375 Randerbuch, K. 31 Rand-Meir, T. 29, 31 Ranney, H. M. 315, 316, 334 Rao, S. T. 272 Raval, D. 171 Ravilly, A. 107 Ray, W. J., Jr. 534 Redfield, A. G. 349, 397,399,

402,405--411,552, 558 Reed, C. S. 306 Reed, G. H. 533-540 Reed, L .J . 199,203 Reed, M. L. 221 Reeke, G. N. 272, 273, 277-

284, 526 Reich, E. 263, 264, 266, 268 Reichard, P. 285 Reichmann, M. E. 469, 470,

477-479 Reimann, J. E. 82 Reissmann, K. R. 316 Rental, R. 313 Requena, Y. 3, 10, 71 Reuben, J. 14, 533-536, 553,

558 Reynolds, D. A. 462 Reynolds, J. A. 177 Reynolds, S. J. 151,152, 162 Reynolds, W. L. 407 Rich, A. 184 Richards, F. M. 35-43, 87,

92, 93, 107, 108, 118, 142, 180, 221,245,248, 375, 382, 389, 526, 545, 562, 577, 578

Rickli, E. E. 221 Riddiford, L. M. 225 Riddle, B. 7, 9, 10 Rieder, S. V. 157, 158, 160,

161 Rieke, W. O. 277 Rigbi, M. 145-147 Riggs, A. 268, 306, 312, 316,

322, 326, 332, 354-356 Riordan, J. F. 517-531, 566 Roberts, G. C. K. 48,257,

535 Roberts, J. D. 13 Robertson, R. E. 582 Robertus, J. D. 107,

117-123 Rose, I. A. 152, 153, 157,

158, 160-163 Rosemeyer, M. A. 308 Rosenberg, A. 225 Rosenkrantz, H. 145 Rosenzwieg, N. 512 Rossi, C. 221 Rossi, G. 421 Rossi, G. L. 64, 80, 82, 107 Rossi-Bernardi, L. 311-313 Rossi-Fanelli, A. 343, 349

NAME INDEX 643

Rossmann, M. G. 174, 179- 191, 229, 277, 288, 371, 414, 469--488, 496, 506

Rottmann, F. M. 37 Roughton, F. J. w . 221,

227,239 Rovery, M. 71 Roy, D. 469 Rozantsev, E. G. 325 Rubin, M. M. 295 Rubinstein, M. 552, 556 Ruhlmann, A. 141-150 Rumen, N. M. 354, 356 Rupley, J. A. 29, 107,524 Russell, W. C. 505 Ryd6n, L. 469-488 Ryle, A. P. 233

S

Sachs, L. 271,277 Saito, K. 514 Sakore, T. D. 263-270 Salahuddin, A. 514 Salmeen, I. 409, 410 Salvesen, K. 9 Sampath Narayanan, A. 96 Sanger, F. 233 Sarma, R. H. 188, 413-419 Sarma, V. R. 427,482 Saroff, H. A. 346 Sasisekharan, V. 142, 375,

376, 575 Sauvage, J. P. 115 Scatchard, G. 326 Schachman, H. K. 285. Scatturin, A. 37 Schaub, M. C. 205 Schechter, A. N. 249-252,

254 Schecter, I. 87, 96, 119 Scheele, R. B. 455 Schejter, A. 402 Scheler, W. 355 Schellenberg, K. A. 179,

188 Schelhnan, C. 526 Schelhnan, J. A. 253, 518,

526 Scheraga, H. A. 253,513 Schevitz, R. Vr 179-191 Schiflter, M. 271-276,

427-432 Schillinger, W. E. 551,552,

554, 558, 566 Schimmel, P. R. 162 Schlesinger, M. J. 177 Schlichtkrull, J. 233 Schirmer, R. H. 538 Schmidt, K. 480 Schneider, F. 221 Schneider, W. 477 Schoellmann, G. 86 Schoenborn, B. P. 569-575 Scholtan, W. 145 Schramm, G. 449 Schramm, H. J. 148 Schultz, F. 149 Schunn, R. A. 383,384 Schwert, G. W. 179, 188,

189, 565 Scopes, R. K. 166, 170 Scouloudi, H. 349 Sealock, R. W. 146, 147

Secemski, I. I. 45-51 Segal, D. M. 64, 85-90, 99-

101, 117, 122, 131, 585 Selbin, J. 48 Semancik, J. S. 462 Shapiro, B. M. 291 Sharkey, M. M. 277 Sharon, N. 29 Shaw, E. 86, 120 Shaw, E. N. 517,519 Sheard, B. 541 Sheppard, G. 29 Sherman, M. P. 145 Shethna, Y. I. 369 Shifrin, S. 188 Shimizu, A. 316 Shimizu, K. 329, 547 Shiro, M. 48 Shoham, J. 271,277 Shotton, D. M. 67, 88,

91-105, 129, 133, 189 Shulman, R. G. 56, 57, 307,

326, 330, 332,337-341, 346, 409, 410, 533,551, 554, 557

Sieker, L. C. 359-367 Sigler, P: B. 63, 71, 85, 91,

93, 95, 125 Sillen, L. G. 54 Silverton, E. W. 413-419 Simpson, P. G. 506 Simpson, R. T. 520, 521 Simon, H. 158 Simon, S. R. 316, 317, 325 Singer, B. 459, 462 Singer, S. J. 517 Slater, E. C. 193 Sluyterman, L. A. 107 Smiley, I. E. 179-191 Snfillie, L. B. 205 Smillie, R. M. 369 Smith, D. W. 56 Smith, H. O. 268, 269 Smith, K. O. 507 Smith, L. F. 239 So, L. L. 271,277 Sobatka, H. 522 Sobel, B. E. 359, 381 Sobell, H. M. 263-270 Sokolovsky, M. 145 Solomon, A. 427 Solomon, I. 552, 556 Sparks, R. A. 370 Spatz, L. 387, 393, 394 Sperling, R. 513 Spilburg, C. A. 343-348 Spoek, G. 344 St. Pierre, T. 4 Stabinger, H. 477 Stadtman, E. R. 291 Stamatoyannopoulos, G.

315,322 Stammers, D. K. 165--170 Stannard, J. N. 402 Stark, G. R. 285,286 Steffen, R. M. 511,512 Steigemann, W. 141-150,

351 Stein, W. D. 40 Steitz, T. A. 63, 64, 66, 85,

87, 100, 101, 121, 131, 147, 166, 522, 562, 563, 592

Stengle, T. R. 511 Stern, H. S. 514 Sternlicht, H. 537 Stevens, C. L. 449, 455 Stevens, F. C. 145 Stewart, J. M. 365

Storm, D. R. 13-20, 21, 25 Strahs, G. 381,383,388 Strandberg, B. 221-231, 440,

469-488 Strittmatter, P. 387, 390,

393-395 Stroud, R. M. 91, 96,

125-140, 147 Stroup, S. R. 225 Sturtevant, J. M. 21, 24 Stryer, L. 511,527,535 Studebaker, J. 551-559,

561-567 Stynes, H. 344, 347 Sundberg, H. 477 Suelter, C. H. 169, 534 Sumner, J. B. 271,272, 274,

277,283 Sundaralingam, M. 184, 190 Svedberg, T. H. E. 350, 354 Sykes, B. D. 29-33, 47 Swanson, R. 397-404 Swift, T. J. 533 Szent-Gyorgyi, A. G. 205,

216

T

Tabachnick, M. 522 Tagawa, K. 381 Tahmisian, T. N. 430 Takano, S. 58, 397-404,

405,410, 411 Tamburro, A. M. 37 Tanaka, N. 378 Tandon, S. G. 49 Tanford, C. 36, 257,514 Taniuchi, H. 243, 249-255 Tashian, R. E. 221,225,229 Tashjian, Z. H. 76, 78, 79 Tao, T. 496 Taylor, J. S. 227,535 TenEyck, L. F. 116,

295-310, 321 Terrey, H. 514 Terry, W. D. 413-419 Theorell, H. 107,402 Thielmann, H. 257-261 Thomas, A. V. 253 Thompson, R. C. 96, 97, I00 Thorne, C. 171 Tilander, B. 221,225 Timasheff, S. N. 85,223 Tinoco, I. 526 Tobias, P. 148 Tobin, A. J. 221 Tollin, G. 375, 377, 378 Tollin, P. 472 Tomita, S. 303,326, 332 Topper, Y. J. 157 Traub, A. C. 579 Travis, J. 129 Trentham, D. R. 102, 162,

286 Trueblood, K. N. 265 Truffa-Bachi, P. 197 Tsernoglou, D. 171-178 Tsugita, A. 387, 391, 395 Tulinsky, A. 131 Turner, A. 14, 24, 26 Twinn, K. E. 436 Tyuma, I. 303, 329, 337,

547

U

Ulmer, D. D. 61,402 Usher, D. A. 42, 48 Uyeda, K. 166 Uyemoto, J. K. 469

V

Valentine, R. C. 291-294, 417,503,505

Vallee, B. L. 53, 61,366, 517-531, 551,554, 564

Vanaman, T. C. 285,286 Van der Helm, D. 220 Vand, V, 433 Vandlen, R. L. 13l Velick, S. 188, 197,387 Venable, J. H. 238 Vennesland, B. 179 Verpoorte, J. A. 566 Vetter, H. 369 Victor, T. A. 265 Vinogradov, S. 356 Vishnu 5 Visser, L. 102 Vithayathil, P. J. 37 Vogel, R. 141 yon Glehn, M. 378 von Sengbusch, P. 433--448

W

Waara, I. 221-231, 470, 477 Wacker, W. E. C. 519 Wade, M. 171, 172, 175, 176 Wade-Jardetzky, N. G. 257,

258 Wald, G. 354 Waley, S. G. 151, 157, 161 Walsh, K. A. 88, 125 Walter, P. 171 Wang, J. H. 5, 9, 66, 163,

346 Wang, J. L. 283,284 Wang, T-W. 141 Warburg, O. 168 Ward, K. B. 349-357 Waring, M. 263,264 Warren, S. G. 285-290 Wasserman, P. M. 180, 188 Watenpaugh, K. D. 58, 60,

359-367 Waterfield, M. 218 Watson, H. C. 91-105, 125,

]g5-170, 189, 245,297, 351, 363,393,421,429, 432, 569, 575,585, 586

Watson, J. D. 433,435,473, 589

Waxdal, M. J. 283,284 Waygood, E. R. 221 Webb, E. C. 50, 161 Weber, B. H. 291-294 Weber, K. 206, 285,479,

480, 482, 491,495 Wedler, F. 291-294 Wei, C. H. 383, 384 Weiner, H. 325 Wells, P. R. 4

644 NAME INDEX

Wells, R. D. 263, 264, 266, 267

Wendell, P. L. 165-170 Werner, P. 503-510 Wemham, C. 56, 59 Westheimer, F .H . 48, 591 Westmoreland, D. G.

511-516 Wheland, G. W. 78 Whitaker, J. R. 563 White, N. J. 91-105 Whitehead, E. 193 Whiteley, H. R. 360 Whitney, P. L. 225,229 Wilcox, P. E. 85-90, 117-123 Wiley, D. C. 285-290 Williams, A. 2, 4, 6, 8 Williams, C. H. 370 Williams, M. N. 257-261

Williams, R. C. 462 Williams, R. J. P. 53-62,

163, 299, 366, 519, 521 Willoughby, T. V. 220 Wilson, K. A. 147 Wilson, S. 240 Wirtz, A. J. 221 wit tmann, H. G. 438, 448,

461 Woenckhaus, C. 179, 187 Wold, F. 169 Wolfe, R. 171 Wolfenden, R. 45, 47, 51,

152-154, 591 Wood, M. K. 271-276,

427-432 Woods, E. F. 205, 215 Woods, R. D. 469 Woodward, R. B. 13

Woolfolk, C. A. 291 Wooten, J. F. 311,312, 321,

547 Wright, C. S. 63-70, 95, 107-

109, 113, 116, 117, 121,147, 189, 223

Wu, C. W. 194 Wiithrich, K. 399, 405, 407,

4O8, 541 Wyckoff, H. W. 35-43, 107,

223,272, 277,370, 371, 430, 433, 442

Wyman, J. 313, 353, 547

X

Xuong, N. H. 288, 381-385

Y

Yamashita, T. 84 Yanari, S. 563, 564 Yang, P. C. 179, 188, 189 Yankeelov, J. A. 585-587 Yariv, J. 271,277 Yasunobu, K. T. 360, 375,

376 Yates, R. A. 285 Yonetani, T. 59 Yoshida, A. 315

Z

Zeppezauer, M. 370, 427 Zerner, B. 78, 88, 147, 148 Zillig, W. 449 Zito, R. 349

two-color stereo diagrams -...

Documents