Protein Stability If the egg white protein, ovalbumin, is denatured in a hard-boiled egg, then which of the following is least affected? The quaternary structure of ovalbumin The primary structure of ovalbumin The secondary structure of ovalbumin The tertiary structure of ovalbumin The quaternary structure of ovalbumin The primary structure of ovalbumin The secondary structure of ovalbumin The tertiary structure of ovalbumin ANSWER DOWNLOAD EXAMIANS APP
Protein Stability At the midpoint of a temperature transition curve, Keq = 1.0 and ΔG = 0 half of the protein is denatured All of these [Native] = [Unfolded] Keq = 1.0 and ΔG = 0 half of the protein is denatured All of these [Native] = [Unfolded] 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 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 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 unfolding is favored enthalpically the entropy is negative at all temperatures folding is favored enthalpically the entropy is positive at all temperatures unfolding is favored enthalpically the entropy is negative at all temperatures ANSWER DOWNLOAD EXAMIANS APP
Protein Stability Attractive Vander Waals forces occur between only if other forces are less favorable any pair of nearby atoms apolar molecules in the liquid state polar molecules in the solid state only if other forces are less favorable any pair of nearby atoms apolar molecules in the liquid state polar molecules in the solid state 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 13-15 other amino acids 1-3 other amino acids 5-7 other amino acids 9-12 other amino acids 13-15 other amino acids 1-3 other amino acids 5-7 other amino acids ANSWER DOWNLOAD EXAMIANS APP
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