PROTEIN STABILITY QUIZ

Conformational entropy

Hydrophobic interactions

Electrostatic interactions

Vander Waals interactions

apolar molecules in the liquid state

any pair of nearby atoms

only if other forces are less favorable

polar molecules in the solid state

Keq = 1.0 and ΔG = 0

[Native] = [Unfolded]

All of these

half of the protein is denatured

folding is favored enthalpically

the entropy is negative at all temperatures

the entropy is positive at all temperatures

unfolding is favored enthalpically

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

All hydrophobic amino acids are buried when a protein folds

Tyrosine is only found in the interior of proteins

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

only on Pro residues

only at the ends of a-helices

rarely

only at the turns connecting p-strands

The secondary structure of ovalbumin

The tertiary structure of ovalbumin

The primary structure of ovalbumin

The quaternary structure of ovalbumin

reflects the reduction in solvent-accessible area during protein folding

is similar to effects seen with SDS denaturation

is only meaningful for the polar amino acids

ignores the important contribution of the peptide bond

Hydrogen bonds

Vander Waals interactions

Conformational entropy

Hydrophobic Interactions

1-3 other amino acids

5-7 other amino acids

13-15 other amino acids

9-12 other amino acids