Protein Stability
Which of the following forces is the most favorable for protein folding?

Conformational entropy
Vander Waals interactions
Hydrophobic Interactions
Hydrogen bonds

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Protein Stability
Since ΔG° = -RTlnK

a 10-fold decrease in K increases ΔG° by about 10-fold
a 10-fold decrease in K decreases ΔG° by about 2.3*RT
a 10-fold increase in K decreases ΔG° by about 2.3*RT
a 10-fold increase in K decreases ΔG° by about 10-fold

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Protein Stability
The correlation between free energy ΔG transfer between the aqueous/organic phases and the surface area of amino acid residues

reflects the reduction in solvent-accessible area during protein folding
is only meaningful for the polar amino acids
ignores the important contribution of the peptide bond
is similar to effects seen with SDS denaturation

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