Protein Stability Buried hydrophobic side chains in a globular protein fit into a hole formed by the side chains of 13-15 other amino acids 9-12 other amino acids 5-7 other amino acids 1-3 other amino acids 13-15 other amino acids 9-12 other amino acids 5-7 other amino acids 1-3 other amino acids ANSWER DOWNLOAD EXAMIANS APP
Protein Stability Which of the following is the most correct? Charged amino acids are never buried in the interior of a protein Tyrosine is only found in the interior of proteins Charged amino acids are seldom buried in the interior of a protein All hydrophobic amino acids are buried when a protein folds Charged amino acids are never buried in the interior of a protein Tyrosine is only found in the interior of proteins 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 Attractive Vander Waals forces occur between polar molecules in the solid state any pair of nearby atoms apolar molecules in the liquid state only if other forces are less favorable polar molecules in the solid state any pair of nearby atoms apolar molecules in the liquid state only if other forces are less favorable 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 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 is only meaningful for the polar amino acids ignores the important contribution of the peptide bond 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 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 The secondary structure of ovalbumin 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
EXAMIANS