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
Protein Stability Which of the following forces is the most unfavorable for protein folding? Vander Waals interactions Hydrophobic interactions Conformational entropy Electrostatic interactions Vander Waals interactions Hydrophobic interactions Conformational entropy Electrostatic interactions 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 on Pro residues rarely only at the ends of a-helices only at the turns connecting p-strands only on Pro residues rarely only at the ends of a-helices ANSWER DOWNLOAD EXAMIANS APP
Protein Stability Attractive Vander Waals forces occur between polar molecules in the solid state any pair of nearby atoms only if other forces are less favorable apolar molecules in the liquid state polar molecules in the solid state any pair of nearby atoms only if other forces are less favorable apolar molecules in the liquid state ANSWER DOWNLOAD EXAMIANS APP
Protein Stability The correlation between free energy ΔG transfer between the aqueous/organic phases and the surface area of amino acid residues ignores the important contribution of the peptide bond is only meaningful for the polar amino acids reflects the reduction in solvent-accessible area during protein folding is similar to effects seen with SDS denaturation ignores the important contribution of the peptide bond is only meaningful for the polar amino acids reflects the reduction in solvent-accessible area during protein folding is similar to effects seen with SDS denaturation 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
EXAMIANS