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 13-15 other amino acids 1-3 other amino acids 5-7 other amino acids 9-12 other amino acids 13-15 other amino acids 1-3 other amino acids 5-7 other amino acids ANSWER DOWNLOAD EXAMIANS APP
Protein Stability Attractive Vander Waals forces occur between polar molecules in the solid state apolar molecules in the liquid state any pair of nearby atoms only if other forces are less favorable polar molecules in the solid state apolar molecules in the liquid state any pair of nearby atoms only if other forces are less favorable ANSWER DOWNLOAD EXAMIANS APP
Protein Stability Which of the following forces is the most unfavorable for protein folding? Vander Waals interactions Hydrophobic interactions Electrostatic interactions Conformational entropy Vander Waals interactions Hydrophobic interactions Electrostatic interactions Conformational entropy ANSWER DOWNLOAD EXAMIANS APP
Protein Stability Which of the following is the most correct? Charged amino acids are never buried in the interior of a protein Tyrosine is only found in the interior of proteins Charged amino acids are seldom buried in the interior of a protein All hydrophobic amino acids are buried when a protein folds Charged amino acids are never buried in the interior of a protein Tyrosine is only found in the interior of proteins 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 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 is similar to effects seen with SDS denaturation ignores the important contribution of the peptide bond is only meaningful for the polar amino acids reflects the reduction in solvent-accessible area during protein folding is similar to effects seen with SDS denaturation ignores the important contribution of the peptide bond ANSWER DOWNLOAD EXAMIANS APP
Protein Stability At the midpoint of a temperature transition curve, 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 half of the protein is denatured [Native] = [Unfolded] ANSWER DOWNLOAD EXAMIANS APP
EXAMIANS