Organic 25: Amino Acids, Peptides, & Proteins Flashcards
Amino acids
carboxylic acids that contain an amine function
Peptide bond
an amide bond between the carboxylic acid function of 1 amino acid and the amino nitrogen of another forms this type of bond
Dipeptide
molecule consisting of 2 amino acids joined by a peptide bond
Tripeptide
molecule consisting of 3 amino acids joined by 2 peptide bonds
Tetrapeptide
molecule consisting of 4 amino acids joined by 3 peptide bonds
Polypeptides
peptides with more then 30-50 amino acids
Proteins
polypeptides that have some biological function
Standard amino acids
group of 20 amino acids coded for in DNA-directed protein synthesis; all are alpha-amino acids; all but one contain a primary amino function
Essential amino acids
amino acids that must be obtained from one’s diet
Amino Acid Racemization (AAR)
novel technique for dating archaeological samples; based on the stereochemistry of amino acids
Zwitterion
the form in which neutral amino acids actually exist; the amino group is in its protonated form and the carboxyl group is present as a carboxylate
Isoelectric (isoionic) point
pH at which the amino acid has no net charge
N (amino) terminus
the left end of the peptide, contains the amino group
C (carboxyl) terminus
the right end of the peptide, containing the carboxyl group
Amino acid residues
individual amino acid components of peptides
Primary structure
amino acid sequence plus any disulfide links
Peptidases
the enzymes that catalyze the hydrolysis of peptide bonds
Peptide map
the collection of sequenced fragments of amino acids for a particular substance
Edman Degradation
method for determining the N-terminal amino acid of a peptide or protein; involves treating the material with phenyl isothiocyanate (C6H5N=C=S), cleaving with acid, then identifying the phenylthiohydantoin (PTH derivative) produced
Secondary structure
conformational relationship of nearest neighbor amino acids with respect to each other
Alpha helix, Beta sheet
secondary structures of proteins
Random coils
a portion of a protein that lacks an ordered secondary structure
Tertiary structure
the way a protein chain is folded; affects both its physical properties and its biological function
Fibrous
protein bundles of elongated filaments of protein chains; insoluble in water
Globular
spherical proteins; either soluble or form colloidal dispersions in water
Hydrophobic effect
the excluding of nonpolar molecules from water
Enzyme
a protein that catalyzes a chemical reaction in a living system
Active site
region of an enzyme at which a substrate is bound
Cofactors
a molecule that acts in combination with an enzyme to bring about a reaction; may either be a coenzyme or a prosthetic group
Coenzyme
cofactors that are organic molecules and not covalently bonded to the enzyme
Prosthetic group
cofactors that are organic molecules and ARE covalently bonded to the enzyme
Quaternary structure
description of the way in which 2 or more protein chains, not connected by chemical bonds, are organized in a larger protein