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 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 13-15 other amino acids 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 Attractive Vander Waals forces occur between any pair of nearby atoms polar molecules in the solid state apolar molecules in the liquid state only if other forces are less favorable any pair of nearby atoms polar molecules in the solid state apolar molecules in the liquid state only if other forces are less favorable ANSWER DOWNLOAD EXAMIANS APP
Protein Stability Since ΔG° = -RTlnK 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 10-fold a 10-fold increase in K decreases ΔG° by about 2.3*RT 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 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 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 For the unfolding reaction of Protein G, ΔH° =210.6 kJ/mol, this means that the entropy is positive at all temperatures the entropy is negative at all temperatures folding is favored enthalpically unfolding is favored enthalpically the entropy is positive at all temperatures the entropy is negative at all temperatures folding is favored enthalpically unfolding is favored enthalpically ANSWER DOWNLOAD EXAMIANS APP
EXAMIANS