Protein Stability Buried hydrophobic side chains in a globular protein fit into a hole formed by the side chains of 1-3 other amino acids 5-7 other amino acids 9-12 other amino acids 13-15 other amino acids 1-3 other amino acids 5-7 other amino acids 9-12 other amino acids 13-15 other amino acids 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 folding is favored enthalpically the entropy is positive at all temperatures the entropy is negative at all temperatures unfolding is favored enthalpically folding is favored enthalpically the entropy is positive at all temperatures 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 secondary structure of ovalbumin The tertiary structure of ovalbumin The quaternary structure of ovalbumin The primary structure of ovalbumin The secondary structure of ovalbumin The tertiary structure of ovalbumin The quaternary structure of ovalbumin ANSWER DOWNLOAD EXAMIANS APP
Protein Stability Which of the following forces is the most unfavorable for protein folding? Electrostatic interactions Hydrophobic interactions Conformational entropy Vander Waals interactions Electrostatic interactions Hydrophobic interactions Conformational entropy Vander Waals interactions 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 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 is only meaningful for the polar amino acids ignores the important contribution of the peptide bond is similar to effects seen with SDS denaturation ANSWER DOWNLOAD EXAMIANS APP
Protein Stability Attractive Vander Waals forces occur between 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 polar molecules in the solid state apolar molecules in the liquid state only if other forces are less favorable ANSWER DOWNLOAD EXAMIANS APP
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