Amino Acids, Peptides, and Proteins

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Vocabulary practice flashcards covering core concepts of amino acid chemistry, peptide structure, ionization properties, non-standard amino acids, and protein purification techniques based on Lehninger Principles of Biochemistry.

Last updated 4:11 PM on 9/26/26
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23 Terms

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Keratin

A fibrous structural protein found in all vertebrates that serves as the chief structural component of hair, scales, horns, wool, nails, and feathers.

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<p>Chirality</p>

Chirality

The structural property of an object or molecule that is non-superimposable on its mirror image, as seen in all standard amino acids except glycine.

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Zwitterion

A dipolar molecule containing spatially separated positive and negative charged functional groups, resulting in a net electrical charge of zero.

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Isoelectric Point (pIpI)

The specific pH at which a molecule or protein carries a net charge of zero and does not migrate in an electric field.

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Enantiomers

Nonsuperimposable mirror-image stereoisomers that possess identical physical properties except for the direction in which they rotate plane-polarized light.

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Ibuprofen Enantiomers

Chiral forms of an anti-inflammatory drug where the S(+)S(+)-enantiomer actively inhibits cyclooxygenase (COX), whereas the R(−)R(-)-enantiomer is inactive against COX and is incorporated into triglycerides.

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Cystine

The dimeric amino acid formed when two cysteine residues undergo oxidation to create a covalent disulfide bond.

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Selenocysteine

An uncommon amino acid containing a selenium atom in place of sulfur, inserted into proteins during translation via a specialized UGAUGA stop codon.

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Peptide Bond

A substituted amide linkage formed through a condensation reaction between the \text{\tau-carboxyl} group of one amino acid and the \text{\tau-amino} group of another.

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Cation-Exchange Chromatography

A column purification technique using a solid matrix with negatively charged functional groups to retain positively charged proteins while allowing negatively charged proteins to elute earlier.

<p>A column purification technique using a solid matrix with negatively charged functional groups to retain positively charged proteins while allowing negatively charged proteins to elute earlier.</p>
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Size-Exclusion Chromatography

A separation technique using porous polymer beads through which larger protein molecules elute earlier while smaller molecules enter bead pores and are retarded.

<p>A separation technique using porous polymer beads through which larger protein molecules elute earlier while smaller molecules enter bead pores and are retarded.</p>
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Affinity Chromatography

A column separation method that isolates a target protein based on its specific, non-covalent binding interaction with a polymer-bound ligand.

<p>A column separation method that isolates a target protein based on its specific, non-covalent binding interaction with a polymer-bound ligand.</p>
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Sodium Dodecyl Sulfate (SDS)

An anionic detergent used in gel electrophoresis to denature proteins and impart a uniform negative charge-to-mass ratio, allowing separation solely by molecular weight.

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Isoelectric Focusing

An electrophoretic method that separates proteins within a stationary pH gradient until each protein reaches the region equal to its isoelectric point (pIpI).

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Two-Dimensional (2D) Gel Electrophoresis

A high-resolution analytical technique combining isoelectric focusing in the first dimension (separating by pIpI) with SDS-PAGE in the second dimension (separating by molecular weight MrM_r).

<p>A high-resolution analytical technique combining isoelectric focusing in the first dimension (separating by $$pI$$) with SDS-PAGE in the second dimension (separating by molecular weight $$M_r$$).</p>
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Beer-Lambert Law

The mathematical relationship A = \text{\tau} c l expressing UV-visible light absorbance AA as a linear function of molar absorptivity \text{\tau}, solute concentration cc, and path length ll.

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Specific Activity

The ratio of total enzyme or protein activity units to total protein concentration or mass, serving as a quantitative measure of purity during protein isolation.

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Edman Degradation

A classical chemical sequencing method that labels and cleaves the N-terminal amino acid residue of a peptide using phenylisothiocyanate under basic and acidic conditions.

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Matrix-Assisted Laser Desorption/Ionization (MALDI)

A soft ionization mass spectrometry method where short laser pulses desorb and ionize macromolecules co-crystallized with an light-absorbing chemical matrix.

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Electrospray Ionization (ESI)

A mass spectrometry ionization technique where a high-voltage capillary disperses a liquid protein sample into microdroplets, generating intact gas-phase ions.

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GABA (\text{\tau}-Aminobutyric Acid)

A major inhibitory neurotransmitter in the brain formed via the enzymatic decarboxylation of glutamate.

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Histamine

A amine signaling molecule involved in inflammatory and allergic responses, produced by the decarboxylation of histidine.

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Ornithine

A non-proteinogenic amino acid that serves as a critical metabolic intermediate in the urea cycle and arginine biosynthesis.