Protein Stability The correlation between free energy ΔG transfer between the aqueous/organic phases and the surface area of amino acid residues is similar to effects seen with SDS denaturation reflects the reduction in solvent-accessible area during protein folding ignores the important contribution of the peptide bond is only meaningful for the polar amino acids is similar to effects seen with SDS denaturation reflects the reduction in solvent-accessible area during protein folding ignores the important contribution of the peptide bond is only meaningful for the polar amino acids ANSWER DOWNLOAD EXAMIANS APP
Protein Stability If the egg white protein, ovalbumin, is denatured in a hard-boiled egg, then which of the following is least affected? The primary structure of ovalbumin The quaternary structure of ovalbumin The tertiary structure of ovalbumin The secondary structure of ovalbumin The primary structure of ovalbumin The quaternary structure of ovalbumin The tertiary structure of ovalbumin The secondary structure of ovalbumin 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 negative at all temperatures the entropy is positive at all temperatures unfolding is favored enthalpically folding is favored enthalpically the entropy is negative at all temperatures the entropy is positive at all temperatures unfolding is favored enthalpically 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 Since ΔG° = -RTlnK a 10-fold increase in K decreases ΔG° by about 2.3*RT a 10-fold decrease in K decreases ΔG° by about 2.3*RT a 10-fold decrease in K increases ΔG° by about 10-fold 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 decreases ΔG° by about 2.3*RT a 10-fold decrease in K increases ΔG° by about 10-fold a 10-fold increase in K decreases ΔG° by about 10-fold ANSWER DOWNLOAD EXAMIANS APP
Protein Stability Which of the following is the most correct? Charged amino acids are seldom buried in the interior of a protein Tyrosine is only found in the interior of proteins Charged amino acids are never buried in the interior of a protein All hydrophobic amino acids are buried when a protein folds Charged amino acids are seldom buried in the interior of a protein Tyrosine is only found in the interior of proteins Charged amino acids are never buried in the interior of a protein All hydrophobic amino acids are buried when a protein folds ANSWER DOWNLOAD EXAMIANS APP
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