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

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

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Q. Attractive Vander Waals forces occur between

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

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Q. At the midpoint of a temperature transition curve,

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

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Q. Which of the following is the most correct?

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

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Q. Since ΔG° = -RTlnK

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

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

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Q. In an SDS-PAGE

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Q. Proteins can be visualized directly in gels by

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

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

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

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Q. In a gel filtration column

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

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Q. The subunit molecular weight as well as the number of subunits in the quaternary structure can be determined by

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Q. Proteins are separated in an SDS-PAGE experiment on the basis of their

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