Protein Stability
Unpaired H-bond donors and acceptors are found in the hydrophobic core of a protein

only at the turns connecting p-strands
only on Pro residues
rarely
only at the ends of a-helices

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Protein Stability
The correlation between free energy ΔG transfer between the aqueous/organic phases and the surface area of amino acid residues

reflects the reduction in solvent-accessible area during protein folding
is only meaningful for the polar amino acids
is similar to effects seen with SDS denaturation
ignores the important contribution of the peptide bond

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Protein Stability
Since ΔG° = -RTlnK

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

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Protein Stability
Which of the following is the most correct?

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

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