STRUCTURE AND PROPERTIES OF PEPTIDES QUIZ

Which of the following is an example of tertiary structure in a protein?

A P-pleated sheet

A multimeric protein

A globular domain

An a-helix

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The heme is held in place by a bond between

the Fe3+ and cysteine

the Fe3+ and histidine

the Fe2+ and cysteine

the Fe2+ and histidine

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The Ramachandran Plot illustrates the fact that

the F & Y angles can assume approximately three different values

the peptide bond is planar

the F & Y angles can assume any value in a peptide

the F & Y angles can assume only a single value in a protein

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What is the proportion of glycine residues in collagenous regions?

One-third

One-fourth

One-tenth

Half

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Hemoglobin has quaternary structure and is made up of

four polypeptide chains, two α-chains and two β-chains

two polypeptide chains, one α-chains and one β-chains

five polypeptide chains, two α-chains and three β-chains

six polypeptide chains, two α-chains and four β-chains

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Disulfide bonds most often stabilize the native structure of

hydrophobic proteins

extracellular proteins

dimeric proteins

intracellular proteins

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The different orders of protein structure are determined by all of the following bond types except

peptide bonds

disulfide bridges

hydrogen bonds

phospho-diester bonds

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In the β-pleated sheet

hydrogen bonds are formed between the peptide bonds

All of these

adjacent polypeptide chains can either be parallel or antiparallel

the polypeptide chain is fully extended

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The peptide, Val-Lys-Glu-Met-Ser-Trp-Arg-Ala, was digested with cyanogen bromide (CNBr) to produce:

Val-Lys-Glu-Met + Ser-Trp-Arg-Ala

Val-Lys-Glu + Met-Ser-Trp-Arg-Ala

Val-Lys + Glu-Met-Ser + Trp-Arg-Ala

Val-Lys-Glu-Met-Ser-Trp + Arg-Ala

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Which hemoglobin chain replaces the beta chain in embryonic hemoglobulin?

Delta

Alfa

Gamma

Epsilon

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