PROTEIN STABILITY QUIZ

only if other forces are less favorable

any pair of nearby atoms

polar molecules in the solid state

apolar molecules in the liquid state

The primary structure of ovalbumin

The quaternary structure of ovalbumin

The tertiary structure of ovalbumin

The secondary structure of ovalbumin

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

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

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

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

is similar to effects seen with SDS denaturation

ignores the important contribution of the peptide bond

reflects the reduction in solvent-accessible area during protein folding

is only meaningful for the polar amino acids

only at the ends of a-helices

only on Pro residues

only at the turns connecting p-strands

rarely

Hydrogen bonds

Hydrophobic Interactions

Vander Waals interactions

Conformational entropy

Vander Waals interactions

Electrostatic interactions

Conformational entropy

Hydrophobic interactions

5-7 other amino acids

1-3 other amino acids

9-12 other amino acids

13-15 other amino acids

unfolding is favored enthalpically

folding is favored enthalpically

the entropy is negative at all temperatures

the entropy is positive at all temperatures

half of the protein is denatured

All of these

[Native] = [Unfolded]

Keq = 1.0 and ΔG = 0