Protein Stability Which of the following forces is the most favorable for protein folding? Hydrogen bonds Hydrophobic Interactions Vander Waals interactions Conformational entropy Hydrogen bonds Hydrophobic Interactions Vander Waals interactions 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 reflects the reduction in solvent-accessible area during protein folding is similar to effects seen with SDS denaturation is only meaningful for the polar amino acids ignores the important contribution of the peptide bond reflects the reduction in solvent-accessible area during protein folding is similar to effects seen with SDS denaturation is only meaningful for the polar amino acids ANSWER DOWNLOAD EXAMIANS APP
Protein Stability Which of the following forces is the most unfavorable for protein folding? Vander Waals interactions Conformational entropy Electrostatic interactions Hydrophobic interactions Vander Waals interactions Conformational entropy Electrostatic interactions Hydrophobic interactions ANSWER DOWNLOAD EXAMIANS APP
Protein Stability Attractive Vander Waals forces occur between 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 polar molecules in the solid state ANSWER DOWNLOAD EXAMIANS APP
Protein Stability Since ΔG° = -RTlnK 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 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 ANSWER DOWNLOAD EXAMIANS APP
Protein Stability For the unfolding reaction of Protein G, ΔH° =210.6 kJ/mol, this means that 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 folding is favored enthalpically ANSWER DOWNLOAD EXAMIANS APP
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