PROTEIN STABILITY QUIZ

The primary structure of ovalbumin

The secondary structure of ovalbumin

The quaternary structure of ovalbumin

The tertiary structure of ovalbumin

rarely

only on Pro residues

only at the turns connecting p-strands

only at the ends of a-helices

ignores the important contribution of the peptide bond

is only meaningful for the polar amino acids

is similar to effects seen with SDS denaturation

reflects the reduction in solvent-accessible area during protein folding

the entropy is positive at all temperatures

unfolding is favored enthalpically

folding is favored enthalpically

the entropy is negative at all temperatures

Hydrophobic interactions

Vander Waals interactions

Electrostatic interactions

Conformational entropy

13-15 other amino acids

5-7 other amino acids

9-12 other amino acids

1-3 other amino acids

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

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

Conformational entropy

Hydrogen bonds

Vander Waals interactions

Hydrophobic Interactions

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

Tyrosine is only found in the interior of proteins

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

All hydrophobic amino acids are buried when a protein folds

half of the protein is denatured

[Native] = [Unfolded]

All of these

Keq = 1.0 and ΔG = 0