ap & adv. biology honors needed for class: –3-ring binder (d-rings are best): you might start...
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AP & Adv. Biology Honors
• Needed for Class:– 3-Ring Binder (D-Rings are best): You might start with a 2.5” or
a 3.0” binder. At midterm, you will probably need a second binder of similar size.
– Dividers for Binder, labeled• Daily Journal• Class Notes• Homework/Classwork, Study Guides, Labs• Tests/Quizzes
– Pens/Pencils– Colored Pencils Kept in Binder– Highlighter– White Board Markers (optional)
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Other Items• Logistics:
– Come to class ON TIME– Upon arrival, turn to Daily Journal and answer the day’s question
appropriately. Do not skip any questions.– Remove all items from your desk except binder– No food, snacks, etc.– No cell phones out, in lab, etc. – Keep binder neat and sectioned– Focus: i.e., “Let the dude in the front do your studying”
• Think of YOUR FUTURE. You want to What?__________________• Think College
• How will you succeed there if 90+% of your grade comes from 3-4 Tests?
• If college classes don’t collect homework, then what is the purpose of homework/classwork, etc?
• If there are only 3 tests/Semester, and 12 Chapters are covered per semester, then each test will cover how many chapters?______
• How will you learn that volume of material for the “long-term?”
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• Grading– Tests = 75%
• Are Cumulative
• Later tests in a Term count more than initial tests in the same term, with each term ending with a “Term Exam”
• When will you do your studying for each test?
• How will you remember the material a year from now (Think College)?
– Labs, Study Guides, Homework, Classwork, Binder = 25%• Are not all equal. Some labs are more complex than others, and count more. Same for all other
work.
• Due dates will be clear, and often, work is due on the day of the exam.
• Study Groups?
• AP vs. Honors Levels– AP receives extra readings, extra study guide questions, extra essay and MC
questions on tests, etc.– Honors receives a grade “boost”
• Extra Lab Time/Extra Help Times– Will be Posted a week in advance.
– Get a pass the day before you plan to come in
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Other Items
04/21/23 4
Chapter 2: Basic Chemistry Highlites
Essential Elements of LifeAbout 25 of the 92 elements are essential to lifeCarbon, hydrogen, oxygen, and nitrogen make up 96% of living matterMost of the remaining 4% consists of calcium, phosphorus, potassium, and sulfurTrace elements are those required by an organism in minute quantities
CHNOPS
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Isotopes
• Atoms of an element have the same number of protons but may differ in number of neutrons
• Isotopes are two atoms of an element that differ in number of neutrons• Most isotopes are stable, but some are radioactive, giving off particles
and energy
• Some applications of radioactive isotopes in biological research:– Dating fossils– Tracing atoms through metabolic processes– Diagnosing medical disorders
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LE 2-7b
Third energy level (shell)
Second energy level (shell)
First energy level (shell)
Atomicnucleus
Energyabsorbed
Energylost
04/21/23 7
LE 2-12
H
O
H
H2O+ +
–
Chapter 3: Water and the Fitness of the Environment
– Water is the biological medium here on Earth– All living organisms require water more than any other substance
• Three-quarters of the Earth’s surface is submerged in water
• The abundance of water is the main reason the Earth is habitable
Figure 3.1
• Concept 3.1: The polarity of water molecules results in hydrogen bonding
• The water molecule is a polar molecule
• The polarity of water molecules
– Allows them to form hydrogen bonds with each other
– Contributes to the various properties water exhibits
Hydrogenbonds
+
+
H
H+
+
–
–
– –
Figure 3.2
Qualities of Water that are caused by its polarity and the biological significance of those qualities
• Water molecules exhibit cohesion: Water attracts to water as it hydrogen bonds to itself
• Biological Significance:
• Water has a high specific heat:
• Biological Significance
– Moderate Temperature
– High Heat of Vaporization
– Ice Floats
Qualities of Water that are caused by its polarity and the biological significance of those qualities
Water is a versatile Solvent
• Biological Significance
– Reactions within and outside cells
– Rings of Hydration
– Interacts with Polar Molecules, such as some proteins
– Hydrophilic Materials
– Hydrophobic Materials
Qualities of Water that are caused by its polarity and the biological significance of those qualities
• Dissociation of water molecules leads to acidic and basic conditions that affect living organisms
• Water can dissociate into hydronium ions (H3O)+ and hydroxide ions (OH-)
• Changes in the concentration of these ions can have a great affect on living organisms
H
Hydroniumion (H3O+)
H
Hydroxideion (OH–)
H
H
H
H
H
H
+ –
+
Figure on p. 53 of water dissociating
Results in free H+ ions
Qualities of Water that are caused by its polarity and the biological significance of those qualities
• Acids:
• Bases:
• The pH Scale
• Biological Significance of Acids and Bases
– Transport of hormones in plants
– Alteration of protein structures for
• Activation
• Denaturing
Qualities of Water that are caused by its polarity and the biological significance of those qualities
• If acids and bases are potentially harmful to cells and living things, what prevents harm? Why can a person drink a quart of orange juice without sustaining a lethal change in blood pH?
– The Answer
– Applications
• Swansea Dam
• Lungs and Small Intestine
Chapter 4
Carbon and the Molecular Diversity of Life
• Overview: Carbon—The Backbone of Biological Molecules
• All living organisms
– Are made up of chemicals based mostly on the element carbon
Figure 4.1
• Concept 4.1: Organic chemistry is the study of carbon compounds
• Organic compounds
– Range from simple molecules to colossal ones
• The concept of vitalism– Is the idea that organic compounds arise only within living
organisms– Was disproved when chemists synthesized the compounds in the
laboratory
In 1953, Stanley Miller simulated what were thought to be environmental conditions on the lifeless, primordial Earth. As shown in this recreation, Miller used electrical discharges (simulated lightning) to trigger reactions in a primitive “atmosphere” of H2O, H2, NH3 (ammonia), and CH4 (methane)—some of the gases released by volcanoes.
A variety of organic compounds that play key roles in living cells were synthesized in Miller’s apparatus.
EXPERIMENT
RESULTS
CONCLUSIONOrganic compounds may have been synthesized abiotically on the early Earth, setting the stage for the origin of life. (We will explore this hypothesis in more detail in Chapter 26.)Figure 4.2
• Concept 4.2: Carbon atoms can form diverse molecules by bonding to four other atoms
• Carbon has four valence electrons
• This allows it to form four covalent bonds with a variety of atoms
• The bonding versatility of carbon– Allows it to form many diverse molecules,
including carbon skeletons
(a) Methane
(b) Ethane
(c) Ethene (ethylene)
Molecular Formula
Structural Formula
Ball-and-Stick Model
Space-Filling Model
H
H
H
H
H
H
H
H
H
H
H H
HH
C
C C
C C
CH4
C2H6
C2H4
Name and Comments
Figure 4.3 A-C
• The electron configuration of carbon– Gives it covalent compatibility with many
different elements: i.e., it can bond covalently with many other kinds of atoms.
H O N C
Hydrogen
(valence = 1)
Oxygen
(valence = 2)
Nitrogen
(valence = 3)
Carbon
(valence = 4)
Figure 4.4
Molecular Diversity Arising from Carbon Skeleton Variation
• Carbon chains– Form the skeletons of most organic molecules– Vary in length and shape
HHH
HH
H H H
HH
H
H H H
H H HH H
H
H
H
H
H
H
HH
HH H H H
H HH H
H H H H
H H
H H
HH
HH H
H
H
C C C C C
C C C C C C C
CCCCCCCC
C
CC
CC
C
C
CCC
CC
H
H
H
HH
H
H
(a) Length
(b) Branching
(c) Double bonds
(d) Rings
Ethane Propane
Butane 2-methylpropane(commonly called isobutane)
1-Butene 2-Butene
Cyclohexane Benzene
H H H HH
Figure 4.5 A-D
Hydrocarbons
• Hydrocarbons Are molecules consisting of only carbon and hydrogen– Are found as parts of many of life’s vital organic molecules
(a) A fat molecule (b) Mammalian adipose cells
100 µm
Fat droplets (stained red)
Figure 4.6 A, B
Concept 4.3: Functional groups are the parts of molecules involved in chemical reactions
– Are the chemically reactive groups of atoms within an organic molecule– Give organic molecules distinct properties.
CH3
OH
HO
O
CH3
CH3
OH
Estradiol
Testosterone
Female lion
Male lionFigure 4.9
• Some important functional groups of organic compounds
FUNCTIONALGROUP
STRUCTURE
(may be written HO )
HYDROXYL CARBONYL CARBOXYL
OH
In a hydroxyl group (—OH), a hydrogen atom is bonded to an oxygen atom, which in turn is bonded to the carbon skeleton of the organic molecule. (Do not confuse this functional group with the hydroxide ion, OH–.)
When an oxygen atom is double-bonded to a carbon atom that is also bonded to a hydroxyl group, the entire assembly of atoms is called a carboxyl group (—COOH).
C
O O
C
OH
Figure 4.10
The carbonyl group ( CO) consists of a carbon atom joined to an oxygen atom by a double bond.
Acetic acid, which gives vinegar
its sour tatste
NAME OF
COMPOUNDS
Alcohols (their specific
names usually end in -ol)
Ketones if the carbonyl group is
within a carbon skeleton
Aldehydes if the carbonyl
group is at the end of the
carbon skeleton
Carboxylic acids, or organic
acids
EXAMPLE
Propanal, an aldehyde
Acetone, the simplest ketone
Ethanol, the alcohol
present in alcoholic
beverages
H
H
H
H H
C C OH
H
H
H
HH
H
H
C C H
C
C C
C C C
O
H OH
O
H
H
H H
H O
H
Figure 4.10
• Some important functional groups of organic compounds
The amino group (—NH2) consists of a nitrogen atom bonded to two hydrogen atoms and to the carbon skeleton.
AMINO SULFHYDRYL PHOSPHATE
(may be written HS )
The sulfhydryl group consists of a sulfur atom bonded to an atom of hydrogen; resembles a hydroxyl group in shape.
In a phosphate group, a phosphorus atom is bonded to four oxygen atoms; one oxygen is bonded to the carbon skeleton; two oxygens carry negative charges; abbreviated P . The phosphate group (—OPO3
2–) is an ionized form of a phosphoric acid group (—OPO3H2; note the two hydrogens).
N
H
H
SH
O P
O
OH
OH
Figure 4.10
• Some important functional groups of organic compounds
Because it also has a carboxyl group, glycine is both an amine and a carboxylic acid; compounds with both groups are called amino acids.
Glycine EthanethiolGlycerol phosphate
O
C
HO
C
HH
N
H
H
H
C C SH
H
H H
H
H
OH
C C C O P O
OHHH
OH OH
Figure 4.10
• Some important functional groups of organic compounds
Chapter 5
The Structure and Function of Macromolecules
• Macromolecules
– Are large molecules composed of smaller molecules (polymers)
– Are complex in their structures
Figure 5.1
Concept 5.1: Most macromolecules are polymers, built by joining identical or similar monomers into long chains.
Three of the classes of life’s organic molecules are polymers
– Carbohydrates: Sugars, Starch
– Proteins
– Nucleic acids: DNA, RNA
The Synthesis and Breakdown of Polymers• Monomers form larger molecules by condensation
reactions called dehydration reactions
(a) Dehydration reaction in the synthesis of a polymer
HO H1 2 3 HO
HO H1 2 3 4
H
H2O
Short polymer Unlinked monomer
Longer polymer
Dehydration removes a watermolecule, forming a new bond
Figure 5.2A
• Polymers can disassemble by– Hydrolysis
(b) Hydrolysis of a polymer
HO 1 2 3 H
HO H1 2 3 4
H2O
HHO
Hydrolysis adds a watermolecule, breaking a bond
Figure 5.2B
Sugars• Monosaccharides
– Are the simplest sugars
– Can be used for fuel
– Can be converted into other organic molecules
– Can be combined into polymers
Triose sugars(C3H6O3)
Pentose sugars(C5H10O5)
Hexose sugars(C6H12O6)
H C OH
H C OH
H C OH
H C OH
H C OH
H C OH
HO C H
H C OH
H C OH
H C OH
H C OH
HO C H
HO C H
H C OH
H C OH
H C OH
H C OH
H C OH
H C OH
H C OH
H C OH
H C OH
C OC O
H C OH
H C OH
H C OH
HO C H
H C OH
C O
H
H
H
H H H
H
H H H H
H
H H
C C C COOOO
Ald
os
es
Glyceraldehyde
RiboseGlucose Galactose
Dihydroxyacetone
Ribulose
Ke
tos
es
FructoseFigure 5.3
• Monosaccharides– May be linear– Can form rings (about 65% of the time)
H
H C OH
HO C H
H C OH
H C OH
H C
O
C
H
1
2
3
4
5
6
H
OH
4C
6CH2OH 6CH2OH
5C
HOH
C
H OH
H
2 C
1C
H
O
H
OH
4C
5C
3 C
H
HOH
OH
H
2C
1 C
OH
H
CH2OH
H
H
OHHO
H
OH
OH
H5
3 2
4
(a) Linear and ring forms. Chemical equilibrium between the linear and ring structures greatly favors the formation of rings. To form the glucose ring, carbon 1 bonds to the oxygen attached to carbon 5.
OH3
O H OO
6
1
Figure 5.4
• Disaccharides– Consist of two monosaccharides– Are joined by a glycosidic linkage
• Examples of disaccharides Dehydration reaction in the synthesis of maltose. The bonding of two glucose units forms maltose. The glycosidic link joins the number 1 carbon of one glucose to the number 4 carbon of the second glucose. Joining the glucose monomers in a different way would result in a different disaccharide.
Dehydration reaction in the synthesis of sucrose. Sucrose is a disaccharide formed from glucose and fructose.Notice that fructose,though a hexose like glucose, forms a five-sided ring.
(a)
(b)
H
HO
H
HOH H
OH
O H
OH
CH2OH
H
HO
H
HOH
H
OH
O H
OH
CH2OH
H
O
H
HOH H
OH
O H
OH
CH2OH
H
H2O
H2O
H
H
O
H
HOH
OH
OH
CH2OH
CH2OH HO
OHH
CH2OH
HOH
H
H
HO
OHH
CH2OH
HOH H
O
O H
OHH
CH2OH
HOH H
O
HOH
CH2OH
H HO
O
CH2OH
H
H
OH
O
O
1 2
1 41– 4
glycosidiclinkage
1–2glycosidic
linkage
Glucose
Glucose Glucose
Fructose
Maltose
Sucrose
OH
H
H
Figure 5.5
Polysaccharides• Polysaccharides Are polymers of sugars
– Serve many roles in organisms
• Starch Is a polymer consisting entirely of glucose monomers
– In plants, the starch is amylose or amylopectin, such as in potatoes.
– In animals, the starch is glycogen, stored in the liver and muscles.
Chloroplast Starch
Amylose Amylopectin
1 m
(a) Starch: a plant polysaccharideFigure 5.6
• Glycogen– Consists of glucose monomers– Is the major storage form of glucose in animals
Mitochondria Glycogen granules
0.5 m
(b) Glycogen: an animal polysaccharide
Glycogen
Figure 5.6
Structural Polysaccharides• Cellulose Is a polymer of beta glucose
(c) Cellulose: 1– 4 linkage of glucose monomers
H O
O
CH2OH
HOH H
H
OH
OHH
H
HO
4
C
C
C
C
C
C
H
H
H
HO
OH
H
OH
OH
OH
H
O
CH2OH
HH
H
OH
OHH
H
HO
4 OH
CH2OH
O
OH
OH
HO41
O
CH2OH
O
OH
OH
O
CH2OH
O
OH
OH
CH2OH
O
OH
OH
O O
CH2OH
O
OH
OH
HO4
O1
OH
O
OH OHO
CH2OH
O
OH
O OH
O
OH
OH
(a) and glucose ring structures
(b) Starch: 1– 4 linkage of glucose monomers
1
glucose glucose
CH2OH
CH2OH
1 4 41 1
Figure 5.7 A–C
Plant cells
0.5 m
Cell walls
Cellulose microfibrils in a plant cell wall
Microfibril
CH2OH
CH2OH
OH
OH
OO
OHO
CH2OHO
OOH
OCH2OH OH
OH OHO
O
CH2OH
OO
OH
CH2OH
OO
OH
O
O
CH2OHOH
CH2OHOHOOH OH OH OH
O
OH OH
CH2OH
CH2OH
OHO
OH CH2OH
OO
OH CH2OH
OH
Glucose monomer
O
O
O
O
O
O
Parallel cellulose molecules areheld together by hydrogenbonds between hydroxyl
groups attached to carbonatoms 3 and 6.
About 80 cellulosemolecules associate
to form a microfibril, themain architectural unitof the plant cell wall.
A cellulose moleculeis an unbranched glucose polymer.
OH
OH
O
OOH
Cellulosemolecules
Figure 5.8
– Is a major component of the tough walls that enclose plant cells
• Cellulose is difficult to digest– Cows (and termites) have microbes in their
stomachs to facilitate this process
Figure 5.9
An Animal Structural Polysaccharide
• Chitin, is an important structural polysaccharide in animals– Is found in the exoskeleton of arthropods– Can be used as surgical thread
(a) The structure of the chitin monomer.
O
CH2OH
OHH
H OH
H
NH
CCH3
O
H
H
(b) Chitin forms the exoskeleton of arthropods. This cicada is molting, shedding its old exoskeleton and emergingin adult form.
(c) Chitin is used to make a strong and flexible surgical
thread that decomposes after the wound or incision heals.
OH
Figure 5.10 A–C
Carbohydrates Review
Lipids: Fats, Waxes, Oils
• Concept 5.3: Lipids are a diverse group of hydrophobic molecules
• Lipids Are the one class of large biological molecules that do not consist of polymers– Share the common trait of being hydrophobic
• Fats
– Are constructed from two types of smaller molecules, a single glycerol and usually three fatty acids
Fats
(b) Fat molecule (triacylglycerol)
H HH H
HHH
HH
HH
HH
HH
HOH O HC
C
C
H
H OH
OH
H
HH
HH
HH
HH
HH
HH
HH
H
HCCC
CC
CC
CC
CC
CC
CC C
Glycerol
Fatty acid(palmitic acid)
H
H
H
H
HH
HH
HH
HH
HH
HH
HH
HH
HHHH
HHHHHHHHHHHH
H
HH
H HH
H HH
HH
HH
HH
HH
HHHHHHHHHHH
HH
H
H H H H H H H H HH
HH H H H
H
HH
HHHHHH
HHHHH
HH
HO
O
O
O
OC
C
C C C C C C C C C C C C C C C C C
C
CCCCCCC
CCCCCCCCC
C C C C C C C C C C C CC
CC
O
O
(a) Dehydration reaction in the synthesis of a fatEster linkage
Figure 5.11
• Fatty acids Vary in the length and number and locations of double bonds they contain
• Saturated fatty acids Have the maximum number of hydrogen atoms possible: Have no double bonds
(a) Saturated fat and fatty acid
Stearic acid
Figure 5.12
• Unsaturated fatty acids Have one or more double bonds– Can be converted to saturated via hydrogenation (pump-in
hydrogens), forming trans-fats, or trans-fatty acids.
(b) Unsaturated fat and fatty acidcis double bondcauses bending
Oleic acid
Figure 5.12
Phospholipids• Phospholipids Have only two fatty acids Have a phosphate group instead of
a third fatty acid
• Phospholipid structure Consists of a hydrophilic “head” and hydrophobic “tails”
CH2
O
PO O
O
CH2CHCH2
OO
C O C O
Phosphate
Glycerol
(a) Structural formula (b) Space-filling model
Fatty acids
(c) Phospholipid symbol
Hy
dro
ph
ob
ic t
ail
s
Hydrophilichead
Hydrophobictails
–
Hy
dro
ph
ilic
he
ad CH2 Choline
+
Figure 5.13
N(CH3)3
The structure of phospholipids
– Results in a bilayer arrangement found in cell membranes. They will spontaneously form into this structure when placed in water.
• This happens because water is excluded from the hydrophobic regions and attracted to the hydrophilic.
Hydrophilichead
WATER
WATER
Hydrophobictail
Figure 5.14
Steroids: A type of Lipid (guaranteed answer on this year’s AP Exam!!)
• Steroids Are lipids characterized by a carbon skeleton consisting of four fused rings
• One steroid, cholesterol Is found in cell membranes
– Is a precursor for some hormones
HO
CH3
CH3
H3C CH3
CH3
Figure 5.15
• Concept 5.4: Proteins have many structures, resulting in a wide range of functions– Proteins
• Have many roles inside the cell– Enzymes– Channels, gates, receptors in membranes– Signals (protein kinases)– Transcription Factors– And More!!
• An overview of protein functions
Table 5.1
• Enzymes– Are a type of protein that acts as a catalyst,
speeding up chemical reactions
Substrate(sucrose)
Enzyme (sucrase)
Glucose
OH
H O
H2O
Fructose
3 Substrate is convertedto products.
1 Active site is available for a molecule of substrate, the
reactant on which the enzyme acts.
Substrate binds toenzyme.
22
4 Products are released.
Figure 5.16
Polypeptides
• Polypeptides Are polymers of amino acids• A protein Consists of one or more polypeptides
• Amino acids Are organic molecules possessing both carboxyl and amino groups
– Differ in their properties due to differing side chains, called R groups
• 20 different amino acids make up proteins
O
O–
H
H3N+ C C
O
O–
H
CH3
H3N+ C
H
C
O
O–
CH3 CH3
CH3
C C
O
O–
H
H3N+
CH
CH3
CH2
C
H
H3N+
CH3
CH3
CH2
CH
C
H
H3N+ C
CH3
CH2
CH2
CH3N+
H
C
O
O–
CH2
CH3N+
H
C
O
O–
CH2
NH
H
C
O
O–
H3N+ C
CH2
H2C
H2N C
CH2
H
C
Nonpolar
Glycine (Gly) Alanine (Ala) Valine (Val) Leucine (Leu) Isoleucine (Ile)
Methionine (Met) Phenylalanine (Phe)
C
O
O–
Tryptophan (Trp) Proline (Pro)
H3C
Figure 5.17
S
O
O–
O–
OH
CH2
C C
H
H3N+
O
O–
H3N+
OH CH3
CH
C C
HO–
O
SH
CH2
C
H
H3N+ C
O
O–
H3N+ C C
CH2
OH
H H H
H3N+
NH2
CH2
OC
C C
O
O–
NH2 O
C
CH2
CH2
C CH3N+
O
O–
O
Polar
Electricallycharged
–O O
C
CH2
C CH3N+
H
O
O–
O– O
C
CH2
C CH3N+
H
O
O–
CH2
CH2
CH2
CH2
NH3+
CH2
C CH3N+
H
O
O–
NH2
C NH2+
CH2
CH2
CH2
C CH3N+
H
O
O–
CH2
NH+
NHCH2
C CH3N+
H
O
O–
Serine (Ser) Threonine (Thr)Cysteine
(Cys)Tyrosine
(Tyr)Asparagine
(Asn)Glutamine
(Gln)
Acidic Basic
Aspartic acid (Asp)
Glutamic acid (Glu)
Lysine (Lys) Arginine (Arg) Histidine (His)
Amino Acid Polymers• Amino acids
– Are linked by peptide bondsOH
DESMOSOMES
DESMOSOMESDESMOSOMES
OH
CH2
C
N
H
C
H O
H OH OH
Peptidebond
OH
OH
OH
H H
HH
H
H
H
H
H
H H
H
N
N N
N N
SHSide
chains
SH
OO
O O O
H2O
CH2 CH2
CH2 CH2CH2
C C C C C C
C CC C
Peptidebond
Amino end(N-terminus)
Backbone
(a)
Figure 5.18 (b) Carboxyl end(C-terminus)
Determining the Amino Acid Sequence of a Polypeptide
• The amino acid sequences of polypeptides is CRITICAL!!– Were first determined using chemical means– Can now be determined by automated machines
• A protein’s specific conformation
– Determines how it functions
• Two models of protein conformation
(a) A ribbon model
(b) A space-filling model
Groove
Groove
Figure 5.19
Four Levels of Protein Structure
• Primary structure– Is the unique sequence of amino acids in a
polypeptide
Figure 5.20–
Amino acid
subunits
+H3NAmino
end
oCarboxyl end
oc
GlyProThrGlyThr
Gly
GluSeuLysCysProLeu
MetVal
Lys
ValLeu
AspAlaValArgGly
SerPro
Ala
Gly
lleSerProPheHisGluHis
Ala
GluValValPheThrAla
Asn
AspSer
GlyProArg
ArgTyrThr
lleAla
Ala
Leu
LeuSer
ProTyrSerTyrSerThrThr
AlaVal
ValThrAsnProLysGlu
ThrLys
SerTyrTrpLysAlaLeu
GluLleAsp
O C helix
pleated sheet
Amino acidsubunits NC
H
C
O
C N
H
CO H
R
C NH
C
O H
C
R
N
HH
R C
O
R
C
H
NH
C
O H
NCO
R
C
H
NH
H
C
R
C
O
C
O
C
NH
H
R
C
C
O
N
HH
C
R
C
O
NH
R
C
H C
ON
HH
C
R
C
O
NH
R
C
H C
ON
HH
C
R
C
O
N H
H C R
N HO
O C N
C
RC
H O
CHR
N H
O C
RC
H
N H
O CH C R
N H
CC
N
R
H
O C
H C R
N H
O C
RC
H
H
C
RN
H
CO
C
NH
R
C
H C
O
N
H
C
• Secondary structure– Is the folding or coiling of the polypeptide into a
repeating configuration– Includes the helix and the pleated sheet
H H
Figure 5.20
• Tertiary structure
– Is the overall three-dimensional shape of a polypeptide
– Results from interactions between amino acids and R groups
CH2CH
OH
O
CHO
CH2
CH2 NH3+ C-O CH2
O
CH2SSCH2
CH
CH3
CH3
H3C
H3C
Hydrophobic interactions and van der Waalsinteractions
Polypeptidebackbone
Hyrdogenbond
Ionic bond
CH2
Disulfide bridge
• Quaternary structure– Is the overall protein structure that results from
the aggregation of two or more polypeptide subunits
Polypeptidechain
Collagen Chains
ChainsHemoglobin
IronHeme
But What Holds all this Together??
Peptide Bonds
Sulf-hydryl groups form di-sulfide bridges
Hydrogen bonds
Van der Waals forces
Hydrophobic interactions
If you remove all but the peptides, you lose the 2’, 3’, and 4’.
Remove the peptides, lose it all.
Sickle-Cell Disease: A Simple Change in Primary Structure
Primary structure
Secondaryand tertiarystructures
Quaternary structure
Function
Red bloodcell shape
Hemoglobin A
Molecules donot associatewith oneanother, eachcarries oxygen.
Normal cells arefull of individualhemoglobinmolecules, eachcarrying oxygen
10 m 10 m
Primary structure
Secondaryand tertiarystructures
Quaternary structure
Function
Red bloodcell shape
Hemoglobin S
Molecules interact with one another tocrystallize into a fiber, capacity to carry oxygen is greatly reduced.
subunit subunit
1 2 3 4 5 6 7 3 4 5 6 721
Normal hemoglobin Sickle-cell hemoglobin. . .. . .
Figure 5.21
Exposed hydrophobic
region
Val ThrHis Leu Pro Glul Glu Val His Leu Thr Pro Val Glu
What Determines Protein Conformation?
• Protein conformation Depends on the physical and chemical conditions of the protein’s environment
• Denaturation Is when a protein unravels and loses its native conformation (notice the improper usage in this phrase? Good to avoid it).
Denaturation
Renaturation
Denatured proteinNormal protein
Figure 5.22
The Protein-Folding Problem• Most proteins Probably go through several intermediate states on
their way to a stable conformation • Chaperonins Are protein molecules that assist in the proper folding of other
proteins
Hollowcylinder
Cap
Chaperonin(fully assembled)
Steps of ChaperoninAction: An unfolded poly- peptide enters the cylinder from one end.
The cap attaches, causing the cylinder to change shape insuch a way that it creates a hydrophilic environment for the folding of the polypeptide.
The cap comesoff, and the properlyfolded protein is released.
Correctlyfoldedprotein
Polypeptide
2
1
3
Figure 5.23
Some Uses of Proteins
• Antibodies
• Enzymes
• Contractile Proteins
• Gene Regulation
• Receptor Proteins
• Sensory Proteins
• Signal Proteins
• Transport Proteins
• Concept 5.5: Nucleic acids store and transmit hereditary information
• Genes– Are the units of inheritance– Program the amino acid sequence of
polypeptides– Are made of nucleic acids
The Roles of Nucleic Acids
• There are two types of nucleic acids– Deoxyribonucleic acid (DNA)
• Stores information for the synthesis of specific proteins
• Directs RNA synthesis• Directs protein synthesis
through RNA– Ribonucleic acid (RNA)
1
2
3
Synthesis of mRNA in the nucleus
Movement of mRNA into cytoplasm
via nuclear pore
Synthesisof protein
NUCLEUSCYTOPLASM
DNA
mRNA
Ribosome
AminoacidsPolypeptide
mRNA
Figure 5.25
The Structure of Nucleic Acids
• Nucleic acids Exist as polymers called polynucleotides
(a) Polynucleotide, or nucleic acid
3’C
5’ end
5’C
3’C
5’C
3’ endOH
Figure 5.26
O
O
O
O
•Each polynucleotide Consists of monomers called nucleotides
Nitrogenousbase
Nucleoside
O
O
O
O P CH2
5’C
3’CPhosphate
group Pentosesugar
(b) NucleotideFigure 5.26
O
Nucleotide Monomers• Nucleotide monomers
– Are made up of nucleosides and phosphate groups
(c) Nucleoside componentsFigure 5.26
CHCH
Uracil (in RNA)U
Ribose (in RNA)
Nitrogenous bases Pyrimidines
CN
NC
OH
NH2
CHCH
OC
NH
CH
HNC
O
CCH3
N
HNC
C
HO
O
CytosineC
Thymine (in DNA)T
NHC
N C
CN
C
CH
N
NH2 O
NHC
NHH
CC
N
NH
C NH2
AdenineA
GuanineG
Purines
OHOCH2
H
H H
OH
H
OHOCH2
HH H
OH
H
Pentose sugars
Deoxyribose (in DNA) Ribose (in RNA)OHOH
CH
CH
Uracil (in RNA)U
4’
5”
3’OH H
2’
1’
5”
4’
3’ 2’
1’
Nucleotide Polymers
• Nucleotide polymers
Are made up of nucleotides linked by the–OH group on the 3´ carbon of one nucleotide and the phosphate on the 5´ carbon on the next
The sequence of bases along a nucleotide polymer Is unique for each gene
•Cellular DNA molecules Have two polynucleotides that spiral around an imaginary axis and Forms a double helix
• The DNA double helix
– Consists of two antiparallel nucleotide strands
3’ end
Sugar-phosphatebackbone
Base pair (joined byhydrogen bonding)
Old strands
Nucleotideabout to be added to a new strand
A
3’ end
3’ end
5’ end
Newstrands
3’ end
5’ end
5’ end
Itinerary For The Week
• Tues., Wed, Fri. (9/10 – 9/13): Notes: Ch. 2-5
• Thurs-Fri: DO?
• Fri: Thornton Wilder
“It is a far, far better thing that I do, than I have ever done; it is a far, far better rest that I go to than I
have ever known.”
• Readings:– P. 27: Familiarize– 51 – 56– 63 – 66– 68 – 89 (as needed; should be very little)
73
04/21/23 74
Itinerary For The Day
• Sidney Carton, as he comforted a young lady as they both were carted to the guillotine.
• He saved Charles Darnay for Lucy.
• Author????:
Extra Help, Lab Time, Advisory
Date Day of Week Day of Rotation
Times Notes
9/6 Friday 7 9:15 – 1:30
Note: Whenever possible, get a pass the day BEFORE coming, and in ANY case, get a pass. Can’t make one of those times, please see me and we’ll work something out.
Assignments, Tests, and Due Dates
Assignment Due Date
Agar Lab 9/6
Test: Ch. 2-5 ??