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Week 6 Guide
Protein Folding and Unfolding
11
Biochemistry
Undergraduate 4
12/13/2011

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Term
What properties do protein interiors and exteriors have generally?
Definition
Interiors are usually hydrophobic while exteriors are typically hydrophilic.
Term
Does the hydrophobic effect favor folding or unfolding and why?
Definition
Favors protein folding because it frees up the most water molecules.
Term
How much do ionic forces contribute to protein stability?
Definition
Minimally.
Term
What effect does the hydrophobic effect have on volume?
Definition
Minimizes volume through efficient packing.
Term
How do guanidine and urea affect protein stability?
Definition
Act as denaturants.
Term
How would burial of several water molecules in the hydrophobic core influence the entropy of those waters, relative to when those waters are in the bulk solvent?
Definition
Significantly decrease the entropy.
Term
Describe how experiments with RNaseA demonstrate that the
information about how a protein folds is contained within the protein’s sequence.
Definition
When random disulfide bonding occurred, incorrect protein structure resulted showing there was a link between the sequence and tertiary structure.
Term
How are proteins studied using hydrogen exchange?
Definition
Raising the pH does not affect hydrogen bonding in unfolded state but decreases stability of folded state.
Term
How is protein folding studied using stop-flow experiments?
Definition
Fast mixing of denatured protein solution with refolding condition solution and measure Absorbance over time.
Term
How is protein structure studied using NMR?
Definition
2-D NMR's can show placement of atoms to detect protein folding.
Term
How does X-ray crystollagraphy show atom position?
Definition
Through electron density.
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