Protein Stability Which of the following forces is the most favorable for protein folding? Hydrophobic Interactions Conformational entropy Vander Waals interactions Hydrogen bonds Hydrophobic Interactions Conformational entropy Vander Waals interactions Hydrogen bonds ANSWER DOWNLOAD EXAMIANS APP
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 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 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 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 ANSWER DOWNLOAD EXAMIANS APP
Protein Stability Which of the following forces is the most unfavorable for protein folding? Hydrophobic interactions Electrostatic interactions Conformational entropy Vander Waals interactions Hydrophobic interactions Electrostatic interactions Conformational entropy Vander Waals 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 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 The primary structure of ovalbumin The secondary structure of ovalbumin ANSWER DOWNLOAD EXAMIANS APP
Protein Stability Unpaired H-bond donors and acceptors are found in the hydrophobic core of a protein 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 only at the turns connecting p-strands ANSWER DOWNLOAD EXAMIANS APP
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