crash course of biochemistry
TRANSCRIPT
Crash Course in Biochemistry…4 years in 40 min!
Proteins – What are they?
• Not just a dietary concern !• Numerous activities in all organisms:
– Structural & Transport
– Enzymatic (Like Machines -> real nano-tech)
– Signaling & Regulatory– Generalization: Responsible for all rXns. in
your body (ask aud. examples)
Structural Examples• Keratin
– Makes up hair and nails– Disulfide bond hold coil-
coil together– Perm: Break disulfides and
reform them
Structural Examples• Cell Adhesion:
– Helps cells stick
to other cells.
Immunological cells
find their target
• Cytoskeleton:– Protein scaffold to which cellular
components hitch a ride on
Enzymatic Examples• Enzymes run chemical reactions
• Substrate Product
• Usually 1 unique protein for EVERY unique reaction
Enzymatic Examples• Glycolysis:
– Get energy from
breaking down
sugar– Universal
• The Process:– See: http://www.rcsb.org/pdb/molecules/pdb50_1.html
So Many Reactions!
Enzymatic Examples• Notice: Specific protein at every step
• This just a tiny fraction of what we know
• Like a circuit: Where our knowledge of CS is useful
• Drugs: are ways to ‘hack’ the circuit by changing protein behavior– Caffeine– Statins and Cholesterol
Caffeine Example• Epinepherine stimulates production
of cAMP• cAMP increases rate of many rXn’s,
including glycolysis (PFK)• Phosphodiesterase eliminates cAMP• Caffeine is a phosphodiesterase
Inhibitor
Enzymatic + structural example• Muscles: Use ATP to move
Carrier Example• Hemoglobin: Carries Oxygen
Transport Example• Sodium-potassium pump
– Net Effect: push positive charge outside– Electrical field made used for nerve
conduction
What are proteins?• Like magnetic beads on a string
• 20 different beads possible (amino acids)
- The sidechain (R-group) is the difference between the 20 AA’s.
- Hook together like Legos, 1 way to connect
- Backbone repeats
20 Possible Amino Acids• Common to all life
What are proteins?• Regular protein 100-400 AA’s
Protein Folding:
Sidechains attract and repel each other, surround water pushes and pulls (hydrophobic, hydrophilic). This force mashes the protein into a particular shape.
Simulated folding animation:
http://intro.bio.umb.edu/111-112/111F98Lect/folding.html
Protein Structure• Folding results in only 1
conformation (structure or fold)• Sequence determines structure• Structure determines function• Structure VERY important
– Gives insights to how protein works– Cant drive with square wheels– Heat denatures proteins– Digestive Zymogens
• Sequence structure computationally impossible
Structure and Active site• Part of protein where reaction occurs
What if shape different? RuBP won’t bind, No reaction.
Some mutations change critical active site residues.
Genetic Mutations and Disease: sickle cell, PKU
Protein-Protein Docking• Some proteins bind (stick) to each
other in a highly specific way– See hemoglobin
• The final complex is functional• Individual pieces
are not– Toxic truncated
peptides
• RNA polymerase
How are Proteins Made?• DNA is set of instructions (Opcode)
– Bases like
sidechains– A-T G-C– Like many
programs
concatenated
together
Genes…• 1 gene makes 1
protein
• Genes separated
by control regions
• Tells where genes
start and stop
• This still not well
understood
Genes read by RNA polymerase• Regulatory regions attract TF’s,
which attracts RNA poly.
• RNA (single strand) is a
copy of a gene
Ribosome: RNA Protein