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