Protein Stability At the midpoint of a temperature transition curve, [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 All of these 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 secondary structure of ovalbumin The primary structure of ovalbumin The tertiary structure of ovalbumin The quaternary structure of ovalbumin The secondary structure of ovalbumin The primary structure of ovalbumin The tertiary structure of ovalbumin The quaternary 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 at the turns connecting p-strands rarely only at the ends of a-helices only on Pro residues only at the turns connecting p-strands rarely only at the ends of a-helices only on Pro residues ANSWER DOWNLOAD EXAMIANS APP
Protein Stability Which of the following forces is the most unfavorable for protein folding? Vander Waals interactions Hydrophobic interactions Conformational entropy Electrostatic interactions Vander Waals interactions Hydrophobic interactions Conformational entropy Electrostatic interactions ANSWER DOWNLOAD EXAMIANS APP
Protein Stability Which of the following forces is the most favorable for protein folding? Hydrophobic Interactions Vander Waals interactions Hydrogen bonds Conformational entropy Hydrophobic Interactions Vander Waals interactions Hydrogen bonds Conformational entropy 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 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 is similar to effects seen with SDS denaturation is only meaningful for the polar amino acids ANSWER DOWNLOAD EXAMIANS APP
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