Protein Stability Since ΔG° = -RTlnK 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 increase in K decreases ΔG° by about 2.3*RT 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 a 10-fold decrease in K increases ΔG° by about 10-fold a 10-fold increase in K decreases ΔG° by about 2.3*RT a 10-fold decrease in K decreases ΔG° by about 2.3*RT ANSWER DOWNLOAD EXAMIANS APP
Protein Stability Which of the following forces is the most favorable for protein folding? Conformational entropy Hydrophobic Interactions Hydrogen bonds Vander Waals interactions Conformational entropy Hydrophobic Interactions Hydrogen bonds Vander Waals interactions ANSWER DOWNLOAD EXAMIANS APP
Protein Stability If the egg white protein, ovalbumin, is denatured in a hard-boiled egg, then which of the following is least affected? The quaternary structure of ovalbumin The tertiary structure of ovalbumin The secondary structure of ovalbumin The primary structure of ovalbumin The quaternary structure of ovalbumin The tertiary structure of ovalbumin The secondary structure of ovalbumin The primary structure of ovalbumin ANSWER DOWNLOAD EXAMIANS APP
Protein Stability Unpaired H-bond donors and acceptors are found in the hydrophobic core of a protein only on Pro residues rarely only at the ends of a-helices only at the turns connecting p-strands only on Pro residues rarely only at the ends of a-helices only at the turns connecting p-strands ANSWER DOWNLOAD EXAMIANS APP
Protein Stability At the midpoint of a temperature transition curve, All of these [Native] = [Unfolded] Keq = 1.0 and ΔG = 0 half of the protein is denatured All of these [Native] = [Unfolded] Keq = 1.0 and ΔG = 0 half of the protein is denatured ANSWER DOWNLOAD EXAMIANS APP
Protein Stability The correlation between free energy ΔG transfer between the aqueous/organic phases and the surface area of amino acid residues 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 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 ANSWER DOWNLOAD EXAMIANS APP
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