Protein Stability Since ΔG° = -RTlnK 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 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 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 increase in K decreases ΔG° by about 10-fold 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 unfavorable for protein folding? Electrostatic interactions Hydrophobic interactions Vander Waals interactions Conformational entropy Electrostatic interactions Hydrophobic interactions Vander Waals interactions Conformational entropy ANSWER DOWNLOAD EXAMIANS APP
Protein Stability At the midpoint of a temperature transition curve, All of these [Native] = [Unfolded] half of the protein is denatured Keq = 1.0 and ΔG = 0 All of these [Native] = [Unfolded] half of the protein is denatured Keq = 1.0 and ΔG = 0 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 tertiary structure of ovalbumin The primary structure of ovalbumin The secondary structure of ovalbumin The quaternary structure of ovalbumin The tertiary structure of ovalbumin The primary structure of ovalbumin The secondary structure of ovalbumin The quaternary structure of ovalbumin ANSWER DOWNLOAD EXAMIANS APP
Protein Stability Buried hydrophobic side chains in a globular protein fit into a hole formed by the side chains of 9-12 other amino acids 5-7 other amino acids 1-3 other amino acids 13-15 other amino acids 9-12 other amino acids 5-7 other amino acids 1-3 other amino acids 13-15 other amino acids 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 similar to effects seen with SDS denaturation is only meaningful for the polar amino acids reflects the reduction in solvent-accessible area during protein folding ignores the important contribution of the peptide bond is similar to effects seen with SDS denaturation is only meaningful for the polar amino acids reflects the reduction in solvent-accessible area during protein folding ignores the important contribution of the peptide bond ANSWER DOWNLOAD EXAMIANS APP
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