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 For the unfolding reaction of Protein G, ΔH° =210.6 kJ/mol, this means that folding is favored enthalpically unfolding is favored enthalpically the entropy is positive at all temperatures the entropy is negative at all temperatures folding is favored enthalpically unfolding is favored enthalpically the entropy is positive at all temperatures the entropy is negative at all temperatures 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
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 The correlation between free energy ΔG transfer between the aqueous/organic phases and the surface area of amino acid residues reflects the reduction in solvent-accessible area during protein folding is similar to effects seen with SDS denaturation ignores the important contribution of the peptide bond is only meaningful for the polar amino acids reflects the reduction in solvent-accessible area during protein folding is similar to effects seen with SDS denaturation ignores the important contribution of the peptide bond is only meaningful for the polar amino acids ANSWER DOWNLOAD EXAMIANS APP
Protein Stability Buried hydrophobic side chains in a globular protein fit into a hole formed by the side chains of 5-7 other amino acids 13-15 other amino acids 9-12 other amino acids 1-3 other amino acids 5-7 other amino acids 13-15 other amino acids 9-12 other amino acids 1-3 other amino acids ANSWER DOWNLOAD EXAMIANS APP
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