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 rarely only on Pro residues only at the ends of a-helices only at the turns connecting p-strands rarely only on Pro residues 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 Tyrosine is only found in the interior of proteins All hydrophobic amino acids are buried when a protein folds Charged amino acids are seldom buried in the interior of a protein Charged amino acids are never buried in the interior of a protein Tyrosine is only found in the interior of proteins All hydrophobic amino acids are buried when a protein folds Charged amino acids are seldom buried in the interior of a protein ANSWER DOWNLOAD EXAMIANS APP
Protein Stability Which of the following forces is the most favorable for protein folding? Vander Waals interactions Hydrophobic Interactions Conformational entropy Hydrogen bonds Vander Waals interactions Hydrophobic Interactions Conformational entropy Hydrogen bonds ANSWER DOWNLOAD EXAMIANS APP
Protein Stability Buried hydrophobic side chains in a globular protein fit into a hole formed by the side chains of 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 9-12 other amino acids 5-7 other amino acids 13-15 other amino acids ANSWER DOWNLOAD EXAMIANS APP
Protein Stability Which of the following forces is the most unfavorable for protein folding? Vander Waals interactions Electrostatic interactions Conformational entropy Hydrophobic interactions Vander Waals interactions Electrostatic interactions Conformational entropy Hydrophobic interactions 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
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