Protein Stability Which of the following forces is the most unfavorable for protein folding? Electrostatic interactions Conformational entropy Vander Waals interactions Hydrophobic interactions Electrostatic interactions Conformational entropy Vander Waals interactions Hydrophobic interactions ANSWER DOWNLOAD EXAMIANS APP
Protein Stability Which of the following is the most correct? 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 Charged amino acids are never buried in the interior of a protein ANSWER DOWNLOAD EXAMIANS APP
Protein Stability Attractive Vander Waals forces occur between polar molecules in the solid state apolar molecules in the liquid state any pair of nearby atoms only if other forces are less favorable polar molecules in the solid state apolar molecules in the liquid state any pair of nearby atoms only if other forces are less favorable ANSWER DOWNLOAD EXAMIANS APP
Protein Stability Unpaired H-bond donors and acceptors are found in the hydrophobic core of a protein rarely only on Pro residues only at the ends of a-helices only at the turns connecting p-strands rarely only on Pro residues only at the ends of a-helices only at the turns connecting p-strands 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 reflects the reduction in solvent-accessible area during protein folding is only meaningful for the polar amino acids is similar to effects seen with SDS denaturation ignores the important contribution of the peptide bond reflects the reduction in solvent-accessible area during protein folding is only meaningful for the polar amino acids is similar to effects seen with SDS denaturation ignores the important contribution of the peptide bond ANSWER DOWNLOAD EXAMIANS APP
Protein Stability Which of the following forces is the most favorable for protein folding? Hydrogen bonds Hydrophobic Interactions Conformational entropy Vander Waals interactions Hydrogen bonds Hydrophobic Interactions Conformational entropy Vander Waals interactions ANSWER DOWNLOAD EXAMIANS APP
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