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 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 the entropy is positive at all temperatures unfolding is favored enthalpically the entropy is negative at all temperatures folding is favored enthalpically the entropy is positive at all temperatures unfolding is favored enthalpically ANSWER DOWNLOAD EXAMIANS APP
Protein Stability Attractive Vander Waals forces occur between only if other forces are less favorable polar molecules in the solid state apolar molecules in the liquid state any pair of nearby atoms only if other forces are less favorable polar molecules in the solid state apolar molecules in the liquid state any pair of nearby atoms ANSWER DOWNLOAD EXAMIANS APP
Protein Stability Which of the following forces is the most favorable for protein folding? Vander Waals interactions Hydrophobic Interactions Conformational entropy Hydrogen bonds Vander Waals interactions Hydrophobic Interactions Conformational entropy Hydrogen bonds ANSWER DOWNLOAD EXAMIANS APP
Protein Stability At the midpoint of a temperature transition curve, All of these Keq = 1.0 and ΔG = 0 half of the protein is denatured [Native] = [Unfolded] All of these Keq = 1.0 and ΔG = 0 half of the protein is denatured [Native] = [Unfolded] ANSWER DOWNLOAD EXAMIANS APP
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