Q. Disulfide bonds most often stabilize the native structure of

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Q. Secondary structure in protein refers to

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Q. Heme is the binding pocket of myoglobin and hemoglobin and is composed of

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Q. What is the effect of a decrease in pH on hemoglobin oxygen affinity?

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Q. What is the proportion of glycine residues in collagenous regions?

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Q. An oil drop with a polar coat is a metaphor referring to the three dimensional structure of

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Q. What was the first protein whose complete tertiary structure was determined?

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Q. The peptide bond in proteins is

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Q. In β-pleated sheet structures neighbouring

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

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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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