Protein Stability Which of the following is the most correct? Tyrosine is only found in the interior of proteins Charged amino acids are never buried in the interior of a protein Charged amino acids are seldom 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 never buried in the interior of a protein Charged amino acids are seldom buried in the interior of a protein All hydrophobic amino acids are buried when a protein folds 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 At the midpoint of a temperature transition curve, half of the protein is denatured [Native] = [Unfolded] Keq = 1.0 and ΔG = 0 All of these half of the protein is denatured [Native] = [Unfolded] 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 tertiary structure of ovalbumin The secondary structure of ovalbumin The quaternary structure of ovalbumin The primary structure of ovalbumin The tertiary structure of ovalbumin The secondary structure of ovalbumin The quaternary structure of ovalbumin The primary structure of ovalbumin ANSWER DOWNLOAD EXAMIANS APP
Protein Stability Which of the following forces is the most favorable for protein folding? Hydrophobic Interactions Hydrogen bonds Vander Waals interactions Conformational entropy Hydrophobic Interactions Hydrogen bonds Vander Waals interactions 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 is similar to effects seen with SDS denaturation reflects the reduction in solvent-accessible area during protein folding ignores the important contribution of the peptide bond is only meaningful for the polar amino acids is similar to effects seen with SDS denaturation reflects the reduction in solvent-accessible area during protein folding ignores the important contribution of the peptide bond is only meaningful for the polar amino acids ANSWER DOWNLOAD EXAMIANS APP
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