Protein Stability For the unfolding reaction of Protein G, ΔH° =210.6 kJ/mol, this means that unfolding is favored enthalpically the entropy is positive at all temperatures folding is favored enthalpically the entropy is negative at all temperatures unfolding is favored enthalpically the entropy is positive at all temperatures folding is favored enthalpically the entropy is negative at all temperatures ANSWER DOWNLOAD EXAMIANS APP
Protein Stability Attractive Vander Waals forces occur between only if other forces are less favorable any pair of nearby atoms polar molecules in the solid state apolar molecules in the liquid state only if other forces are less favorable any pair of nearby atoms polar molecules in the solid state apolar molecules in the liquid state 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
Protein Stability Which of the following forces is the most unfavorable for protein folding? Electrostatic interactions Vander Waals interactions Hydrophobic interactions Conformational entropy Electrostatic interactions Vander Waals interactions Hydrophobic interactions Conformational entropy ANSWER DOWNLOAD EXAMIANS APP
Protein Stability Unpaired H-bond donors and acceptors are found in the hydrophobic core of a protein 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 only at the turns connecting p-strands ANSWER DOWNLOAD EXAMIANS APP
Protein Stability At the midpoint of a temperature transition curve, half of the protein is denatured All of these Keq = 1.0 and ΔG = 0 [Native] = [Unfolded] half of the protein is denatured All of these Keq = 1.0 and ΔG = 0 [Native] = [Unfolded] ANSWER DOWNLOAD EXAMIANS APP
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