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 1-3 other amino acids 5-7 other amino acids 9-12 other amino acids 13-15 other amino acids 1-3 other amino acids 5-7 other amino acids ANSWER DOWNLOAD EXAMIANS APP
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 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 For the unfolding reaction of Protein G, ΔH° =210.6 kJ/mol, this means that unfolding is favored enthalpically the entropy is negative at all temperatures the entropy is positive at all temperatures folding is favored enthalpically unfolding is favored enthalpically the entropy is negative at all temperatures the entropy is positive at all temperatures folding is favored enthalpically ANSWER DOWNLOAD EXAMIANS APP
Protein Stability Attractive Vander Waals forces occur between polar molecules in the solid state only if other forces are less favorable any pair of nearby atoms apolar molecules in the liquid state polar molecules in the solid state only if other forces are less favorable any pair of nearby atoms apolar molecules in the liquid state ANSWER DOWNLOAD EXAMIANS APP
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
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