Protein Stability Which of the following is the most correct? Charged amino acids are seldom buried in the interior of a protein Charged amino acids are never buried in the interior of a protein Tyrosine is only found in the interior of proteins All hydrophobic amino acids are buried when a protein folds Charged amino acids are seldom buried in the interior of a protein Charged amino acids are never buried in the interior of a protein Tyrosine is only found in the interior of proteins All hydrophobic amino acids are buried when a protein folds 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
Protein Stability Unpaired H-bond donors and acceptors are found in the hydrophobic core of a protein only on Pro residues only at the turns connecting p-strands only at the ends of a-helices rarely only on Pro residues only at the turns connecting p-strands only at the ends of a-helices rarely 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 secondary structure of ovalbumin The quaternary structure of ovalbumin The tertiary structure of ovalbumin The primary structure of ovalbumin The secondary structure of ovalbumin The quaternary structure of ovalbumin The tertiary structure of ovalbumin The primary structure of ovalbumin ANSWER DOWNLOAD EXAMIANS APP
Protein Stability Which of the following forces is the most favorable for protein folding? Hydrogen bonds Hydrophobic Interactions Conformational entropy Vander Waals interactions Hydrogen bonds Hydrophobic Interactions Conformational entropy Vander Waals interactions ANSWER DOWNLOAD EXAMIANS APP
Protein Stability For the unfolding reaction of Protein G, ΔH° =210.6 kJ/mol, this means that the entropy is negative at all temperatures unfolding is favored enthalpically the entropy is positive at all temperatures folding is favored enthalpically the entropy is negative at all temperatures unfolding is favored enthalpically the entropy is positive at all temperatures folding is favored enthalpically ANSWER DOWNLOAD EXAMIANS APP
EXAMIANS