Protein Stability Unpaired H-bond donors and acceptors are found in the hydrophobic core of a protein only at the turns connecting p-strands rarely only on Pro residues only at the ends of a-helices only at the turns connecting p-strands rarely only on Pro residues only at the ends of a-helices ANSWER DOWNLOAD EXAMIANS APP
Protein Stability Which of the following forces is the most favorable for protein folding? Conformational entropy Hydrophobic Interactions Vander Waals interactions Hydrogen bonds Conformational entropy Hydrophobic Interactions Vander Waals interactions Hydrogen bonds 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 only meaningful for the polar amino acids ignores the important contribution of the peptide bond is similar to effects seen with SDS denaturation reflects the reduction in solvent-accessible area during protein folding is only meaningful for the polar amino acids ignores the important contribution of the peptide bond is similar to effects seen with SDS denaturation reflects the reduction in solvent-accessible area during protein folding ANSWER DOWNLOAD EXAMIANS APP
Protein Stability Which of the following forces is the most unfavorable for protein folding? Vander Waals interactions Conformational entropy Hydrophobic interactions Electrostatic interactions Vander Waals interactions Conformational entropy Hydrophobic interactions Electrostatic interactions 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 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 ANSWER DOWNLOAD EXAMIANS APP
Protein Stability For the unfolding reaction of Protein G, ΔH° =210.6 kJ/mol, this means that the entropy is positive at all temperatures the entropy is negative at all temperatures folding is favored enthalpically unfolding is favored enthalpically the entropy is positive at all temperatures the entropy is negative at all temperatures folding is favored enthalpically unfolding is favored enthalpically ANSWER DOWNLOAD EXAMIANS APP
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