Protein Stability Unpaired H-bond donors and acceptors are found in the hydrophobic core of a protein only on Pro residues rarely only at the ends of a-helices only at the turns connecting p-strands only on Pro residues rarely 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 the entropy is positive at all temperatures folding is favored enthalpically unfolding is favored enthalpically the entropy is negative at all temperatures the entropy is positive at all temperatures folding is favored enthalpically unfolding is favored enthalpically the entropy is negative at all temperatures ANSWER DOWNLOAD EXAMIANS APP
Protein Stability Attractive Vander Waals forces occur between 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 polar molecules in the solid state ANSWER DOWNLOAD EXAMIANS APP
Protein Stability Which of the following forces is the most favorable for protein folding? Hydrogen bonds Hydrophobic Interactions Conformational entropy Vander Waals interactions Hydrogen bonds Hydrophobic Interactions Conformational entropy Vander Waals interactions ANSWER DOWNLOAD EXAMIANS APP
Protein Stability At the midpoint of a temperature transition curve, Keq = 1.0 and ΔG = 0 All of these [Native] = [Unfolded] half of the protein is denatured Keq = 1.0 and ΔG = 0 All of these [Native] = [Unfolded] half of the protein is denatured ANSWER DOWNLOAD EXAMIANS APP
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