Protein Stability For the unfolding reaction of Protein G, ΔH° =210.6 kJ/mol, this means that 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 the entropy is negative at all temperatures ANSWER DOWNLOAD EXAMIANS APP
Protein Stability Which of the following forces is the most favorable for protein folding? Hydrophobic Interactions Hydrogen bonds Conformational entropy Vander Waals interactions Hydrophobic Interactions Hydrogen bonds Conformational entropy Vander Waals interactions ANSWER DOWNLOAD EXAMIANS APP
Protein Stability Buried hydrophobic side chains in a globular protein fit into a hole formed by the side chains of 1-3 other amino acids 9-12 other amino acids 13-15 other amino acids 5-7 other amino acids 1-3 other amino acids 9-12 other amino acids 13-15 other amino acids 5-7 other amino acids 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 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 similar to effects seen with SDS denaturation is only meaningful for the polar amino acids reflects the reduction in solvent-accessible area during protein folding ignores the important contribution of the peptide bond is similar to effects seen with SDS denaturation is only meaningful for the polar amino acids reflects the reduction in solvent-accessible area during protein folding ANSWER DOWNLOAD EXAMIANS APP
Protein Stability Which of the following is the most correct? All hydrophobic amino acids are buried when a protein folds Tyrosine is only found in the interior of proteins Charged amino acids are seldom buried in the interior of a protein Charged amino acids are never buried in the interior of a protein All hydrophobic amino acids are buried when a protein folds Tyrosine is only found in the interior of proteins Charged amino acids are seldom buried in the interior of a protein Charged amino acids are never buried in the interior of a protein ANSWER DOWNLOAD EXAMIANS APP
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