UV LUMINANCE SPECTROSCOPY QUIZ

Electrostatic interactions

Hydrophobic interactions

Conformational entropy

Vander Waals interactions

All hydrophobic amino acids are buried when a protein folds

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

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

Tyrosine is only found in the interior of proteins

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

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

unfolding is favored enthalpically

the entropy is negative at all temperatures

the entropy is positive at all temperatures

folding is favored enthalpically

only on Pro residues

only at the ends of a-helices

only at the turns connecting p-strands

rarely

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

is only meaningful for the polar amino acids

only if other forces are less favorable

apolar molecules in the liquid state

any pair of nearby atoms

polar molecules in the solid state

13-15 other amino acids

1-3 other amino acids

5-7 other amino acids

9-12 other amino acids

half of the protein is denatured

Keq = 1.0 and ΔG = 0

[Native] = [Unfolded]

All of these

Hydrogen bonds

Hydrophobic Interactions

Conformational entropy

Vander Waals interactions