Protein Stability At the midpoint of a temperature transition curve, All of these half of the protein is denatured Keq = 1.0 and ΔG = 0 [Native] = [Unfolded] All of these half of the protein is denatured Keq = 1.0 and ΔG = 0 [Native] = [Unfolded] ANSWER DOWNLOAD EXAMIANS APP
Protein Stability Buried hydrophobic side chains in a globular protein fit into a hole formed by the side chains of 13-15 other amino acids 9-12 other amino acids 1-3 other amino acids 5-7 other amino acids 13-15 other amino acids 9-12 other amino acids 1-3 other amino acids 5-7 other amino acids ANSWER DOWNLOAD EXAMIANS APP
Protein Stability Attractive Vander Waals forces occur between any pair of nearby atoms polar molecules in the solid state only if other forces are less favorable apolar molecules in the liquid state any pair of nearby atoms polar molecules in the solid state only if other forces are less favorable apolar molecules in the liquid state 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 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 Unpaired H-bond donors and acceptors are found in the hydrophobic core of a protein 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 rarely ANSWER DOWNLOAD EXAMIANS APP
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