Exam 2: Protein Composition and Structure

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Describe some of the features of an α helix.

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The α helix is a coil stabilized by intrachain hydrogen bonds between the carbonyl oxygen of a residue and the amide hydrogen of the fourth residue away. There are 3.6 amino acids per turn. The hydrogen bonds are between amino acid residues that have three intervening residues. Thus, these amino acid residues are found on the same side of the coil. The helix is almost always right-handed, although left-handed helices are, in theory, possible.

What do the amino acids Tyr, Asn, and Thr have in common?

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E

What are some of the modifications that proteins acquire?

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D

What is the charged group(s) present in glycine at a pH of 7?

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In the ribonuclease experiments performed by Anfinsen, what was the significance of the presence of the reducing agent β-mercaptoethanol?

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What does the modification involving the attachment of acetyl groups to the amino termini of proteins do?

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Which two amino acids contain a sulfur atom?

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How does a protein's amino acid sequence influence the tertiary structure?

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Which amino acid side chains are capable of ionization?

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In the following peptide, which amino acid is the N-terminus? Phe-Ala-Gly-Arg

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What is the "hydrophobic effect" as it relates to protein structure?

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Which of the following is most often found in proteins?

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A protein is considered to be __________________ when it is converted into a randomly coiled structure without its normal activity.

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What are prions?

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Which of the following amino acids has an ionizable R-group with a pKa near neutral pH?

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What is the approximate mass of a protein containing 200 amino acids? (Assume there are no other protein modifications.)

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_______________ is a fibrous protein and is the primary component of wool and hair.

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Key properties of proteins include

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What is the advantage of having 20 different amino acids available to form proteins?

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What is the advantage of protein interaction and assembly with other proteins?

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