PROTEIN STABILITY QUIZ

apolar molecules in the liquid state

polar molecules in the solid state

any pair of nearby atoms

only if other forces are less favorable

13-15 other amino acids

9-12 other amino acids

1-3 other amino acids

5-7 other amino acids

Electrostatic interactions

Conformational entropy

Vander Waals interactions

Hydrophobic interactions

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

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

The secondary structure of ovalbumin

The tertiary structure of ovalbumin

The primary structure of ovalbumin

The quaternary structure of ovalbumin

the entropy is positive at all temperatures

the entropy is negative at all temperatures

unfolding is favored enthalpically

folding is favored enthalpically

All of these

[Native] = [Unfolded]

Keq = 1.0 and ΔG = 0

half of the protein is denatured

Tyrosine is only found in the interior of proteins

Charged amino acids are seldom buried in the interior of a protein

Charged amino acids are never buried in the interior of a protein

All hydrophobic amino acids are buried when a protein folds

Vander Waals interactions

Conformational entropy

Hydrogen bonds

Hydrophobic Interactions

is only meaningful for the polar amino acids

ignores the important contribution of the peptide bond

reflects the reduction in solvent-accessible area during protein folding

is similar to effects seen with SDS denaturation