Protein Stability If the egg white protein, ovalbumin, is denatured in a hard-boiled egg, then which of the following is least affected? The secondary structure of ovalbumin The tertiary structure of ovalbumin The primary structure of ovalbumin The quaternary structure of ovalbumin The secondary structure of ovalbumin The tertiary structure of ovalbumin The primary structure of ovalbumin The quaternary structure of ovalbumin ANSWER DOWNLOAD EXAMIANS APP
Protein Stability Since ΔG° = -RTlnK a 10-fold decrease in K decreases ΔG° by about 2.3*RT a 10-fold increase in K decreases ΔG° by about 10-fold a 10-fold increase in K decreases ΔG° by about 2.3*RT a 10-fold decrease in K increases ΔG° by about 10-fold a 10-fold decrease in K decreases ΔG° by about 2.3*RT a 10-fold increase in K decreases ΔG° by about 10-fold a 10-fold increase in K decreases ΔG° by about 2.3*RT a 10-fold decrease in K increases ΔG° by about 10-fold ANSWER DOWNLOAD EXAMIANS APP
Protein Stability At the midpoint of a temperature transition curve, 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 half of the protein is denatured ANSWER DOWNLOAD EXAMIANS APP
Protein Stability Attractive Vander Waals forces occur between apolar molecules in the liquid state polar molecules in the solid state any pair of nearby atoms only if other forces are less favorable apolar molecules in the liquid state polar molecules in the solid state any pair of nearby atoms only if other forces are less favorable 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 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 9-12 other amino acids 5-7 other amino acids 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 reflects the reduction in solvent-accessible area during protein folding is only meaningful for the polar amino acids is similar to effects seen with SDS denaturation ignores the important contribution of the peptide bond reflects the reduction in solvent-accessible area during protein folding is only meaningful for the polar amino acids is similar to effects seen with SDS denaturation ANSWER DOWNLOAD EXAMIANS APP
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