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 13-15 other amino acids 1-3 other amino acids 9-12 other amino acids 5-7 other amino acids 13-15 other amino acids 1-3 other amino acids ANSWER DOWNLOAD EXAMIANS APP
Protein Stability For the unfolding reaction of Protein G, ΔH° =210.6 kJ/mol, this means that folding is favored enthalpically the entropy is negative at all temperatures the entropy is positive at all temperatures unfolding is favored enthalpically folding is favored enthalpically the entropy is negative at all temperatures the entropy is positive at all temperatures unfolding is favored enthalpically ANSWER DOWNLOAD EXAMIANS APP
Protein Stability Attractive Vander Waals forces occur between polar molecules in the solid state any pair of nearby atoms apolar molecules in the liquid state only if other forces are less favorable polar molecules in the solid state any pair of nearby atoms apolar molecules in the liquid state only if other forces are less favorable ANSWER DOWNLOAD EXAMIANS APP
Protein Stability Which of the following forces is the most favorable for protein folding? Vander Waals interactions Hydrophobic Interactions Hydrogen bonds Conformational entropy Vander Waals interactions Hydrophobic Interactions Hydrogen bonds Conformational entropy 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 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 reflects the reduction in solvent-accessible area during protein folding is similar to effects seen with SDS denaturation 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 only at the turns connecting p-strands only on Pro residues rarely only at the ends of a-helices only at the turns connecting p-strands only on Pro residues rarely ANSWER DOWNLOAD EXAMIANS APP
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