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 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 is similar to effects seen with SDS denaturation reflects the reduction in solvent-accessible area during protein folding ANSWER DOWNLOAD EXAMIANS APP
Protein Stability Attractive Vander Waals forces occur between polar molecules in the solid state apolar molecules in the liquid state only if other forces are less favorable any pair of nearby atoms polar molecules in the solid state apolar molecules in the liquid state only if other forces are less favorable any pair of nearby atoms ANSWER DOWNLOAD EXAMIANS APP
Protein Stability Which of the following is the most correct? Tyrosine is only found in the interior of proteins Charged amino acids are never buried in the interior of a protein Charged amino acids are seldom 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 never buried in the interior of a protein Charged amino acids are seldom buried in the interior of a protein All hydrophobic amino acids are buried when a protein folds 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 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 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 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 folding is favored enthalpically the entropy is positive at all temperatures ANSWER DOWNLOAD EXAMIANS APP
Protein Stability Unpaired H-bond donors and acceptors are found in the hydrophobic core of a protein only on Pro residues only at the ends of a-helices rarely only at the turns connecting p-strands only on Pro residues only at the ends of a-helices rarely only at the turns connecting p-strands ANSWER DOWNLOAD EXAMIANS APP
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