PROTEIN STABILITY QUIZ

Conformational entropy

Electrostatic interactions

Hydrophobic interactions

Vander Waals interactions

All of these

Keq = 1.0 and ΔG = 0

[Native] = [Unfolded]

half of the protein is denatured

The primary structure of ovalbumin

The secondary structure of ovalbumin

The tertiary structure of ovalbumin

The quaternary structure of ovalbumin

any pair of nearby atoms

only if other forces are less favorable

polar molecules in the solid state

apolar molecules in the liquid state

Vander Waals interactions

Conformational entropy

Hydrophobic Interactions

Hydrogen bonds

rarely

only at the turns connecting p-strands

only at the ends of a-helices

only on Pro residues

folding is favored enthalpically

the entropy is positive at all temperatures

the entropy is negative at all temperatures

unfolding is favored enthalpically

13-15 other amino acids

5-7 other amino acids

1-3 other amino acids

9-12 other amino acids

reflects the reduction in solvent-accessible area during protein folding

ignores the important contribution of the peptide bond

is only meaningful for the polar amino acids

is similar to effects seen with SDS denaturation

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

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

a 10-fold increase in K decreases ΔG° by about 10-fold

a 10-fold decrease in K increases ΔG° by about 10-fold