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 the entropy is negative at all temperatures unfolding is favored enthalpically the entropy is positive at all temperatures folding is favored enthalpically the entropy is negative at all temperatures unfolding is favored enthalpically ANSWER DOWNLOAD EXAMIANS APP
Protein Stability Buried hydrophobic side chains in a globular protein fit into a hole formed by the side chains of 9-12 other amino acids 5-7 other amino acids 1-3 other amino acids 13-15 other amino acids 9-12 other amino acids 5-7 other amino acids 1-3 other amino acids 13-15 other amino acids ANSWER DOWNLOAD EXAMIANS APP
Protein Stability Which of the following forces is the most favorable for protein folding? Vander Waals interactions Hydrogen bonds Conformational entropy Hydrophobic Interactions Vander Waals interactions Hydrogen bonds Conformational entropy Hydrophobic 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 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 ANSWER DOWNLOAD EXAMIANS APP
Protein Stability At the midpoint of a temperature transition curve, [Native] = [Unfolded] half of the protein is denatured Keq = 1.0 and ΔG = 0 All of these [Native] = [Unfolded] half of the protein is denatured Keq = 1.0 and ΔG = 0 All of these 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 ignores the important contribution of the peptide bond reflects the reduction in solvent-accessible area during protein folding is similar to effects seen with SDS denaturation is only meaningful for the polar amino acids ignores the important contribution of the peptide bond reflects the reduction in solvent-accessible area during protein folding is similar to effects seen with SDS denaturation ANSWER DOWNLOAD EXAMIANS APP
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