Chapter 3: Amino Acids, Peptides, and Proteins

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Vocabulary flashcards covering amino acid structures, chemical properties, peptide synthesis, titration behavior, and protein characterization techniques.

Last updated 6:29 PM on 9/21/26
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31 Terms

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Amino acid residue

The structure remaining in a peptide chain after two or more amino acids combine and the elements of water are removed during condensation.

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α\alpha-Amino acid

An amino acid containing both an amino group and a carboxylic acid group attached to the primary α\alpha-carbon.

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<p>D,L-System</p>

D,L-System

A configuration system that compares the stereochemistry of chiral molecules to that of glyceraldehyde.

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Glycine

The only achiral amino acid; possesses a small hydrogen side chain that gives it conformational flexibility without contributing hydrophobic interactions.

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Methionine

A nonpolar hydrophobic amino acid containing a thioether side chain that cannot form disulfide bonds.

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Proline

An aliphatic amino acid with a cyclic secondary amino (imino) side group that restricts the conformational flexibility of polypeptide chains.

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<p>Lysine carbon designation</p>

Lysine carbon designation

The system of designating amino acid side-chain carbons sequentially using Greek letters (α,β,γ,δ,ϵ\alpha, \beta, \gamma, \delta, \epsilon) or numbers (11 to 66) starting from the carboxyl carbon.

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<p>Selenocysteine</p>

Selenocysteine

The co-translationally incorporated 21st amino acid; encoded via context-dependent opal suppression and present as 99%99\% deprotonated at neutral pH.

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<p>Pyrrolysine</p>

Pyrrolysine

An amino acid encoded by the amber (UAGUAG) stop codon, first identified in methanogenic archaea.

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<p>Ornithine and Citrulline</p>

Ornithine and Citrulline

Non-protein amino acids that function as key intermediates in arginine biosynthesis and the urea cycle.

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<p>Zwitterion</p>

Zwitterion

A dipolar molecule containing both positively and negatively charged functional groups with an overall net electric charge of zero.

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Amphoteric

The chemical property of a substance (such as an amino acid) enabling it to act as both an acid and a base.

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<p>Isoelectric point ($$pI$$)</p>

Isoelectric point (pIpI)

The specific pH level at which a molecule carries no net electrical charge and is least soluble in water.

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<p>Peptide bond formation</p>

Peptide bond formation

A condensation reaction where the α\alpha-amino group of one amino acid acts as a nucleophile to displace the hydroxyl group of another, releasing a water molecule.

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Oligopeptide

A short peptide chain typically consisting of 4 to 10 amino acid residues.

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Polypeptide

A long chain of amino acid residues joined by peptide bonds, containing more than 10 amino acids.

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<p>L-Aspartyl-L-phenylalanine methyl ester (aspartame)</p>

L-Aspartyl-L-phenylalanine methyl ester (aspartame)

A dipeptide derivative that functions as a synthetic commercial sweetener.

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Multisubunit protein

A protein complex consisting of two or more noncovalently associated polypeptide chains.

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Protomer

An identical repeating structural unit in an oligomeric protein, consisting of one or more polypeptide chains.

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Conjugated protein

A protein that contains permanently attached non-amino acid chemical constituents in addition to polypeptide chains.

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Prosthetic group

A non-amino acid moiety covalently or tightly bound to a conjugated protein required for its biological function.

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Specific activity

The ratio of total enzyme activity units to the total mass of protein in milligrams, used as a measure of protein purity.

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<p>Sodium dodecyl sulfate (SDS)</p>

Sodium dodecyl sulfate (SDS)

An anionic detergent that unfolds proteins and coats them with negative charges to provide uniform mass-to-charge ratios during SDS-PAGE electrophoresis.

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Isoelectric focusing

An electrophoretic technique that separates proteins based on their individual $ pI $ values along an immobilized pH gradient gel.

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Edman degradation

A classical protein sequencing method involving stepwise N-terminal chemical modification, cleavage, and identification of individual amino acid residues.

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Consensus sequence

A calculated order of most frequent amino acid or nucleotide residues found at each position in aligned, related sequences.

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Signature sequence

A conserved motif of 10 to 50 amino acid residues linked to a specific structural fold or biological function in proteins.

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Homologous proteins

Proteins that display detectable sequence similarity due to shared evolutionary origin.

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Paralogs

Homologous proteins encoded by genes arising from gene duplication within the same species.

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Orthologs

Homologous proteins found in different species that evolved from a common ancestral gene.

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Lateral (or Horizontal) gene transfer

The transfer of genetic material between distinct organisms other than through direct vertical offspring transmission.