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