Protein Stability For the unfolding reaction of Protein G, ΔH° =210.6 kJ/mol, this means that 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 the entropy is negative at all temperatures folding is favored enthalpically ANSWER DOWNLOAD EXAMIANS APP
Protein Stability Since ΔG° = -RTlnK a 10-fold decrease in K decreases ΔG° by about 2.3*RT a 10-fold decrease in K increases ΔG° by about 10-fold a 10-fold increase in K decreases ΔG° by about 10-fold a 10-fold increase in K decreases ΔG° by about 2.3*RT a 10-fold decrease in K decreases ΔG° by about 2.3*RT a 10-fold decrease in K increases ΔG° by about 10-fold a 10-fold increase in K decreases ΔG° by about 10-fold a 10-fold increase in K decreases ΔG° by about 2.3*RT 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 is only meaningful for the polar amino acids is similar to effects seen with SDS denaturation ignores the important contribution of the peptide bond reflects the reduction in solvent-accessible area during protein folding is only meaningful for the polar amino acids is similar to effects seen with SDS denaturation ignores the important contribution of the peptide bond reflects the reduction in solvent-accessible area during protein folding ANSWER DOWNLOAD EXAMIANS APP
Protein Stability Attractive Vander Waals forces occur between 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 polar molecules in the solid state any pair of nearby atoms ANSWER DOWNLOAD EXAMIANS APP
Protein Stability At the midpoint of a temperature transition curve, All of these half of the protein is denatured [Native] = [Unfolded] Keq = 1.0 and ΔG = 0 All of these half of the protein is denatured [Native] = [Unfolded] Keq = 1.0 and ΔG = 0 ANSWER DOWNLOAD EXAMIANS APP
Protein Stability Which of the following forces is the most favorable for protein folding? Hydrogen bonds Hydrophobic Interactions Vander Waals interactions Conformational entropy Hydrogen bonds Hydrophobic Interactions Vander Waals interactions Conformational entropy ANSWER DOWNLOAD EXAMIANS APP
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