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 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 ANSWER DOWNLOAD EXAMIANS APP
Protein Stability For the unfolding reaction of Protein G, ΔH° =210.6 kJ/mol, this means that 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 unfolding is favored enthalpically the entropy is positive 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 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 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? Conformational entropy Vander Waals interactions Hydrogen bonds Hydrophobic Interactions Conformational entropy Vander Waals interactions Hydrogen bonds Hydrophobic Interactions ANSWER DOWNLOAD EXAMIANS APP
Protein Stability At the midpoint of a temperature transition curve, All of these Keq = 1.0 and ΔG = 0 [Native] = [Unfolded] half of the protein is denatured All of these Keq = 1.0 and ΔG = 0 [Native] = [Unfolded] half of the protein is denatured ANSWER DOWNLOAD EXAMIANS APP
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