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 13-15 other amino acids 5-7 other amino acids 1-3 other amino acids 9-12 other amino acids 13-15 other amino acids 5-7 other amino acids 1-3 other amino acids ANSWER DOWNLOAD EXAMIANS APP
Protein Stability Since ΔG° = -RTlnK a 10-fold increase in K decreases ΔG° by about 10-fold a 10-fold decrease in K decreases ΔG° by about 2.3*RT a 10-fold decrease in K increases ΔG° by about 10-fold a 10-fold increase in K decreases ΔG° by about 2.3*RT a 10-fold increase in K decreases ΔG° by about 10-fold a 10-fold decrease in K decreases ΔG° by about 2.3*RT a 10-fold decrease in K increases ΔG° by about 10-fold a 10-fold increase in K decreases ΔG° by about 2.3*RT 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 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 The tertiary structure of ovalbumin ANSWER DOWNLOAD EXAMIANS APP
Protein Stability Unpaired H-bond donors and acceptors are found in the hydrophobic core of a protein only at the ends of a-helices rarely only at the turns connecting p-strands only on Pro residues only at the ends of a-helices rarely only at the turns connecting p-strands only on Pro residues 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 similar to effects seen with SDS denaturation ignores the important contribution of the peptide bond is only meaningful for the polar amino acids reflects the reduction in solvent-accessible area during protein folding is similar to effects seen with SDS denaturation ignores the important contribution of the peptide bond is only meaningful for the polar amino acids ANSWER DOWNLOAD EXAMIANS APP
Protein Stability Which of the following forces is the most favorable for protein folding? Conformational entropy Vander Waals interactions Hydrophobic Interactions Hydrogen bonds Conformational entropy Vander Waals interactions Hydrophobic Interactions Hydrogen bonds ANSWER DOWNLOAD EXAMIANS APP
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