Protein Stability If the egg white protein, ovalbumin, is denatured in a hard-boiled egg, then which of the following is least affected? The tertiary structure of ovalbumin The secondary structure of ovalbumin The quaternary structure of ovalbumin The primary structure of ovalbumin The tertiary structure of ovalbumin The secondary structure of ovalbumin The quaternary structure of ovalbumin The primary structure of ovalbumin ANSWER DOWNLOAD EXAMIANS APP
Protein Stability Unpaired H-bond donors and acceptors are found in the hydrophobic core of a protein only at the ends of a-helices only on Pro residues only at the turns connecting p-strands rarely only at the ends of a-helices only on Pro residues only at the turns connecting p-strands rarely ANSWER DOWNLOAD EXAMIANS APP
Protein Stability Attractive Vander Waals forces occur between 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 only if other forces are less favorable any pair of nearby atoms apolar molecules in the liquid state ANSWER DOWNLOAD EXAMIANS APP
Protein Stability Which of the following is the most correct? 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 Charged amino acids are seldom buried in the interior of a protein Tyrosine is only found in the interior of proteins 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 2.3*RT a 10-fold increase in K decreases ΔG° by about 10-fold 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 2.3*RT a 10-fold increase in K decreases ΔG° by about 10-fold a 10-fold decrease in K increases ΔG° by about 10-fold 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 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 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 ANSWER DOWNLOAD EXAMIANS APP
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