Protein Stability Which of the following is the most correct? 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 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 Tyrosine is only found in the interior of proteins 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 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 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 tertiary structure of ovalbumin The primary structure of ovalbumin The quaternary structure of ovalbumin The secondary structure of ovalbumin The tertiary structure of ovalbumin The primary structure of ovalbumin The quaternary structure of ovalbumin ANSWER DOWNLOAD EXAMIANS APP
Protein Stability At the midpoint of a temperature transition curve, half of the protein is denatured [Native] = [Unfolded] All of these Keq = 1.0 and ΔG = 0 half of the protein is denatured [Native] = [Unfolded] All of these Keq = 1.0 and ΔG = 0 ANSWER DOWNLOAD EXAMIANS APP
Protein Stability Which of the following forces is the most favorable for protein folding? Hydrogen bonds Conformational entropy Vander Waals interactions Hydrophobic Interactions Hydrogen bonds Conformational entropy Vander Waals interactions Hydrophobic Interactions ANSWER DOWNLOAD EXAMIANS APP
Protein Stability For the unfolding reaction of Protein G, ΔH° =210.6 kJ/mol, this means that folding is favored enthalpically the entropy is positive at all temperatures unfolding is favored enthalpically the entropy is negative at all temperatures folding is favored enthalpically the entropy is positive at all temperatures unfolding is favored enthalpically the entropy is negative at all temperatures ANSWER DOWNLOAD EXAMIANS APP
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