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 At the midpoint of a temperature transition curve, half of the protein is denatured 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] ANSWER DOWNLOAD EXAMIANS APP
Protein Stability Which of the following forces is the most favorable for protein folding? Vander Waals interactions Hydrophobic Interactions Hydrogen bonds Conformational entropy Vander Waals interactions Hydrophobic Interactions Hydrogen bonds Conformational entropy ANSWER DOWNLOAD EXAMIANS APP
Protein Stability Unpaired H-bond donors and acceptors are found in the hydrophobic core of a protein 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 only at the turns connecting p-strands ANSWER DOWNLOAD EXAMIANS APP
Protein Stability Which of the following forces is the most unfavorable for protein folding? Hydrophobic interactions Vander Waals interactions Conformational entropy Electrostatic interactions Hydrophobic interactions Vander Waals interactions Conformational entropy Electrostatic interactions ANSWER DOWNLOAD EXAMIANS APP
Protein Stability Attractive Vander Waals forces occur between polar molecules in the solid state any pair of nearby atoms apolar molecules in the liquid state only if other forces are less favorable polar molecules in the solid state any pair of nearby atoms apolar molecules in the liquid state only if other forces are less favorable ANSWER DOWNLOAD EXAMIANS APP
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