Protein Stability Which of the following is the most correct? All hydrophobic amino acids are buried when a protein folds Charged amino acids are seldom buried in the interior of a protein Charged amino acids are never buried in the interior of a protein Tyrosine is only found in the interior of proteins All hydrophobic amino acids are buried when a protein folds Charged amino acids are seldom buried in the interior of a protein Charged amino acids are never buried in the interior of a protein Tyrosine is only found in the interior of proteins ANSWER DOWNLOAD EXAMIANS APP
Protein Stability Attractive Vander Waals forces occur between any pair of nearby atoms only if other forces are less favorable polar molecules in the solid state apolar molecules in the liquid state any pair of nearby atoms only if other forces are less favorable polar molecules in the solid state apolar molecules in the liquid state ANSWER DOWNLOAD EXAMIANS APP
Protein Stability Which of the following forces is the most unfavorable for protein folding? Conformational entropy Hydrophobic interactions Electrostatic interactions Vander Waals interactions Conformational entropy Hydrophobic interactions Electrostatic interactions Vander Waals interactions 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 ignores the important contribution of the peptide bond reflects the reduction in solvent-accessible area during protein folding is only meaningful for the polar amino acids is similar to effects seen with SDS denaturation ignores the important contribution of the peptide bond reflects the reduction in solvent-accessible area during protein folding is only meaningful for the polar amino acids is similar to effects seen with SDS denaturation ANSWER DOWNLOAD EXAMIANS APP
Protein Stability Since ΔG° = -RTlnK a 10-fold decrease in K increases ΔG° by about 10-fold a 10-fold increase in K decreases ΔG° by about 10-fold a 10-fold increase in K decreases ΔG° by about 2.3*RT 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 10-fold a 10-fold increase in K decreases ΔG° by about 2.3*RT a 10-fold decrease in K decreases ΔG° by about 2.3*RT ANSWER DOWNLOAD EXAMIANS APP
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