Q. In β-pleated sheet structures neighbouring

View solution

Q. The same peptide, Val-Lys-Glu-Met-Ser-Trp-Arg-Ala. was digested with chymotrypsin to produce

View solution

Q. Unpaired H-bond donors and acceptors are found in the hydrophobic core of a protein

View solution

Q. For the unfolding reaction of Protein G, ΔH° =210.6 kJ/mol, this means that

View solution

Q. Attractive Vander Waals forces occur between

View solution

Q. Which of the following forces is the most favorable for protein folding?

View solution

Q. At the midpoint of a temperature transition curve,

View solution

Q. Buried hydrophobic side chains in a globular protein fit into a hole formed by the side chains of

View solution

Q. Which of the following is the most correct?

View solution

Q. Which of the following forces is the most unfavorable for protein folding?

View solution

Q. Since ΔG° = -RTlnK

View solution

Q. The correlation between free energy ΔG transfer between the aqueous/organic phases and the surface area of amino acid residues

View solution

Q. If the egg white protein, ovalbumin, is denatured in a hard-boiled egg, then which of the following is least affected?

View solution

Q. In an SDS-PAGE

View solution

Q. Proteins can be visualized directly in gels by

View solution

Q. In SDS-PAGE, the protein sample is first

View solution

Q. Electrophoresis of histones and myoglobin under non-denaturing conditions (pH = 7.0) results in

View solution

Q. In isoelectric focusing, proteins are separated on the basis of their

View solution

Q. In a gel filtration column

View solution

Q. In a native PAGE, proteins are separated on the basis of

View solution