Protein Stability At the midpoint of a temperature transition curve, Keq = 1.0 and ΔG = 0 All of these [Native] = [Unfolded] half of the protein is denatured Keq = 1.0 and ΔG = 0 All of these [Native] = [Unfolded] half of the protein is denatured 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 primary structure of ovalbumin The tertiary structure of ovalbumin The quaternary structure of ovalbumin The secondary structure of ovalbumin The primary structure of ovalbumin The tertiary structure of ovalbumin The quaternary structure of ovalbumin The secondary structure of ovalbumin ANSWER DOWNLOAD EXAMIANS APP
Protein Stability Which of the following is the most correct? 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 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 Which of the following forces is the most favorable for protein folding? Hydrophobic Interactions Hydrogen bonds Vander Waals interactions Conformational entropy Hydrophobic Interactions Hydrogen bonds Vander Waals interactions Conformational entropy ANSWER DOWNLOAD EXAMIANS APP
Protein Stability Since ΔG° = -RTlnK 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 increases ΔG° by about 10-fold a 10-fold decrease in K decreases ΔG° by about 2.3*RT 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 increases ΔG° by about 10-fold a 10-fold decrease in K decreases ΔG° by about 2.3*RT ANSWER DOWNLOAD EXAMIANS APP
Protein Stability Unpaired H-bond donors and acceptors are found in the hydrophobic core of a protein 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 only at the ends of a-helices rarely ANSWER DOWNLOAD EXAMIANS APP
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