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24 Cards in this Set
- Front
- Back
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Beta turns
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connect antiparallel β-sheets
4 AA Usually a cis-Proline, and glycine |
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BENDS in polypeptide chains
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- Gly, Ser, Pro, Thr are likely to produce bends
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Functions of
Lysosome Peroxisone Smooth ER Golgi |
Lysome-Hydrolase
Peroxisome- catalase Smooth ER-sterol biosynthesis Golgi-process secretory proteins, glycoslyation |
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Henderson Hasselbalch
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releates pH of solution to the pKa & concentrations of acid & cojugate base
• pH=pKa when [HA] = [A-] |
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Which AA is an imino acid?
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Proline
- Proline has 2 groups on nitrogen |
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Collagen
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3 left handed helices NOT ALPHA --> form Right handed coiled coil
abundant in Gly |
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Silk Fibronin
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Beta sheets High in Ala and Gly
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Keratin
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alpha-Keratin is in alpha-helix
Di-Sulfide bridges important for deratin structure |
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paranitrophenol acetate & imidazole base linked Vs. free in solution is an example of the
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Propinquity Effect
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which is bigger a Protein or Ribosome?
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Ribosome
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peptide bond formation is a __ rx
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condensation
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Enantiomers
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non-super imposable mirror images
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Diastereomers
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contain different stereo centers
if it has n# of stereo centers it has 2-to the n # of diastereomers |
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Gibbs equation
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• ΔG = ΔH – TΔS
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Lance look over AA structures
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aa structures
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AA that binds Biotin
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Lysine
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These are involved in the urea cycle
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Arg & ornithine
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Cofactors
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prosthetic group is a cofactor that is tightly bound
organic or inorganic non-protein. |
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Pyridoxal Phosphate
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Aspartate Transaminase
Transamination business end is an aldehyde (R-CH-C=O) and it forms a Schiff base (R1R2C=N+HR3) with an amine (NH2) of the substrate |
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Anfinsen Experiment
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3 experiments that related enzyme structure to function
ME breaks disulfide bonds urea disrupts hydrophobic interactions |
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Anfinsen Experiment 1
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addition of ME and urea denatured the protein and if these reagents were gradually removed, the protein could in fact renature & regain activity
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Anfinsen Experiment 2
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ME is removed and Urea is still present, the S-S bonds can reform but the hydrophobic interactions remain disrupted so the S-S bonds reform incorrectly, creating a “scrambled ribonuclease" 1% activity
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Anfinsen Experiment 3
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removing the urea and adding trace amounts of ME, so that the S-S bonds could break and reform correctly as urea was removed, allowing the hydrophobic interactions to correctly guide the protein to renature to its active form.
Yes, ribonuclease can be unscrambled |
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Main findings from Anfinsen Experiment
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- the 1o structure (amino acid sequence) contains all of the information for the 3D folded structure’
- this information is not imparted at translation, but in a stepwise manner once all translated - the most thermodynamically stable structure folds - hydrophobic or weak interactions are key to correctly folded proteins - a protein can be renatured (size restraints apply) |
