Protein Stability For the unfolding reaction of Protein G, ΔH° =210.6 kJ/mol, this means that 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 the entropy is positive at all temperatures folding is favored enthalpically ANSWER DOWNLOAD EXAMIANS APP
Protein Stability Which of the following is the most correct? Charged amino acids are never buried in the interior of a protein Tyrosine is only found in the interior of proteins All hydrophobic amino acids are buried when a protein folds Charged amino acids are seldom buried in the interior of a protein Charged amino acids are never buried in the interior of a protein Tyrosine is only found in the interior of proteins All hydrophobic amino acids are buried when a protein folds Charged amino acids are seldom buried in the interior of a protein 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
Protein Stability Attractive Vander Waals forces occur between any pair of nearby atoms polar molecules in the solid state apolar molecules in the liquid state only if other forces are less favorable any pair of nearby atoms polar molecules in the solid state apolar molecules in the liquid state only if other forces are less favorable ANSWER DOWNLOAD EXAMIANS APP
Protein Stability At the midpoint of a temperature transition curve, 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] All of these 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 13-15 other amino acids 1-3 other amino acids 9-12 other amino acids 5-7 other amino acids 13-15 other amino acids 1-3 other amino acids ANSWER DOWNLOAD EXAMIANS APP
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