Protein Stability Unpaired H-bond donors and acceptors are found in the hydrophobic core of a protein only at the turns connecting p-strands only on Pro residues only at the ends of a-helices rarely only at the turns connecting p-strands only on Pro residues only at the ends of a-helices rarely 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 folding is favored enthalpically the entropy is positive at all temperatures the entropy is negative at all temperatures unfolding is favored enthalpically folding is favored enthalpically the entropy is positive at all temperatures the entropy is negative at all temperatures ANSWER DOWNLOAD EXAMIANS APP
Protein Stability Attractive Vander Waals forces occur between 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 only if other forces are less favorable any pair of nearby atoms ANSWER DOWNLOAD EXAMIANS APP
Protein Stability Which of the following forces is the most favorable for protein folding? Hydrogen bonds Hydrophobic Interactions Vander Waals interactions Conformational entropy Hydrogen bonds Hydrophobic Interactions Vander Waals interactions Conformational entropy ANSWER DOWNLOAD EXAMIANS APP
Protein Stability At the midpoint of a temperature transition curve, [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 half of the protein is denatured ANSWER DOWNLOAD EXAMIANS APP