Protein Stability At the midpoint of a temperature transition curve, [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 All of these Keq = 1.0 and ΔG = 0 ANSWER DOWNLOAD EXAMIANS APP
Protein Stability Which of the following forces is the most unfavorable for protein folding? Vander Waals interactions Electrostatic interactions Hydrophobic interactions Conformational entropy Vander Waals interactions Electrostatic interactions Hydrophobic interactions Conformational entropy 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 The correlation between free energy ΔG transfer between the aqueous/organic phases and the surface area of amino acid residues is similar to effects seen with SDS denaturation reflects the reduction in solvent-accessible area during protein folding ignores the important contribution of the peptide bond is only meaningful for the polar amino acids is similar to effects seen with SDS denaturation reflects the reduction in solvent-accessible area during protein folding ignores the important contribution of the peptide bond is only meaningful for the polar amino acids 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 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 unfolding is favored enthalpically ANSWER DOWNLOAD EXAMIANS APP
Protein Stability Which of the following forces is the most favorable for protein folding? Hydrogen bonds Vander Waals interactions Conformational entropy Hydrophobic Interactions Hydrogen bonds Vander Waals interactions Conformational entropy Hydrophobic Interactions ANSWER DOWNLOAD EXAMIANS APP
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