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 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 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 a 10-fold decrease in K increases ΔG° by about 10-fold ANSWER DOWNLOAD EXAMIANS APP
Protein Stability Unpaired H-bond donors and acceptors are found in the hydrophobic core of a protein only on Pro residues rarely only at the turns connecting p-strands only at the ends of a-helices only on Pro residues rarely only at the turns connecting p-strands only at the ends of a-helices 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 folding is favored enthalpically the entropy is negative at all temperatures unfolding is favored enthalpically the entropy is positive at all temperatures folding is favored enthalpically the entropy is negative at all temperatures unfolding is favored enthalpically 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 Which of the following is the most correct? Charged amino acids are never buried in the interior of a protein All hydrophobic amino acids are buried when a protein folds Charged amino acids are seldom buried in the interior of a protein Tyrosine is only found in the interior of proteins Charged amino acids are never buried in the interior of a protein All hydrophobic amino acids are buried when a protein folds Charged amino acids are seldom buried in the interior of a protein Tyrosine is only found in the interior of proteins ANSWER DOWNLOAD EXAMIANS APP
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