Protein Stability Which of the following forces is the most favorable for protein folding? Vander Waals interactions Hydrophobic Interactions Conformational entropy Hydrogen bonds Vander Waals interactions Hydrophobic Interactions Conformational entropy Hydrogen bonds 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 apolar molecules in the liquid state any pair of nearby atoms polar molecules in the solid state only if other forces are less favorable apolar molecules in the liquid state any pair of nearby atoms ANSWER DOWNLOAD EXAMIANS APP
Protein Stability Buried hydrophobic side chains in a globular protein fit into a hole formed by the side chains of 9-12 other amino acids 5-7 other amino acids 13-15 other amino acids 1-3 other amino acids 9-12 other amino acids 5-7 other amino acids 13-15 other amino acids 1-3 other amino acids 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 tertiary structure of ovalbumin The secondary structure of ovalbumin The primary structure of ovalbumin The quaternary structure of ovalbumin The tertiary structure of ovalbumin The secondary structure of ovalbumin The primary 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? Vander Waals interactions Electrostatic interactions Hydrophobic interactions Conformational entropy Vander Waals interactions Electrostatic interactions Hydrophobic interactions Conformational entropy 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 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
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