Exam 5: Proteins: Their Primary Structure and Biological Functions

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The C-terminal residue of a polypeptide can be determined by first cleaving the polypeptide with:

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What is the overall net charge on the peptide lys-lys-ser-glu at pH 7.0?

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α-Helix and β-strand are components of ____ structure

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Explain the significance of the proteome.​

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____ is specific in hydrolyzing only peptide bonds in which the carboxyl function is contributed by an arginine or a lysine residue.

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Proteins with two different polypeptide chains are:

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Insulin is a polypeptide hormone that contains two short polypeptide chains linked by two interstrand disulfide bonds. The most logical order of events to perform in order to sequence this protein would be: A.The peptides are reduced with mercaptoethanol. B.The peptides are sequenced using Edman chemistry. C.The peptides are separated by chromatography techniques. D.The peptides are alkylated with iodoacetamide.

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Which of the following reagents is correctly defined?

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The diversity in hemoglobin mutants indicates that:

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A gene can be defined as:

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Which of the following would be a possible amino acid sequence for an oligopeptide given the experimental data below? 1)The amino acid composition is found to be [ala, lys, phe, met, cys, plus some decomposition products]. 2)The peptide has a molecular weight around 700 Da and absorbs at 280 nm. 3)Treatment with carboxypeptidase results in tryptophan and a peptidE.4.CNBr treatment yields a tetrapeptide and a dipeptidE.5.Trypsin digestion produces an amino acid and a pentapeptide with met on the amino enD.6.Chymotrypsin digestion yields a dipeptide and a tetrapeptidE.

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Proteins that do NOT perform any obvious chemical transformation, but control the ability of other proteins to carry out their physiological functions are:

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Discuss the computer programs that can align amino acid sequences.​

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Membrane proteins differ from globular proteins in that:

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All of the statements about the peptide val-asp-trp-asn-ser are correct EXCEPT:

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The amino acid sequence is NOT:

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After treating a protein with trypsin, which of the following techniques could be used to determine its identity by peptide mass fingerprinting?

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​Explain the role of trypsin in identifying the primary structure of a protein.

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Discuss the quaternary structure of proteins with an example.​

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The advantage of treating separate samples of a protein with two or more enzymes when sequencing a protein is that the products are:

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