Protein Stability Unpaired H-bond donors and acceptors are found in the hydrophobic core of a protein rarely only on Pro residues only at the ends of a-helices only at the turns connecting p-strands rarely only on Pro residues only at the ends of a-helices only at the turns connecting p-strands ANSWER DOWNLOAD EXAMIANS APP
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 any pair of nearby atoms polar molecules in the solid state only if other forces are less favorable apolar molecules in the liquid state any pair of nearby atoms polar molecules in the solid state only if other forces are less favorable apolar molecules in the liquid state ANSWER DOWNLOAD EXAMIANS APP
Protein Stability Which of the following forces is the most favorable for protein folding? Hydrogen bonds Vander Waals interactions Conformational entropy Hydrophobic Interactions Hydrogen bonds Vander Waals interactions Conformational entropy Hydrophobic Interactions ANSWER DOWNLOAD EXAMIANS APP
Protein Stability At the midpoint of a temperature transition curve, [Native] = [Unfolded] All of these half of the protein is denatured Keq = 1.0 and ΔG = 0 [Native] = [Unfolded] All of these half of the protein is denatured Keq = 1.0 and ΔG = 0 ANSWER DOWNLOAD EXAMIANS APP
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