Amino Acids

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39 Terms

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Hydrophobic amino acids

Amino acids that are nonpolar and do not interact well with water.

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Examples of hydrophobic amino acids

Glycine, Alanine, Valine, Leucine, Isoleucine, Methionine, Phenylalanine, Tryptophan, Proline.

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Hydrophilic (polar) amino acids

Amino acids that have side chains that are polar or can form hydrogen bonds with water.

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Examples of hydrophilic amino acids

Serine, Threonine, Cysteine, Tyrosine, Asparagine, Glutamine.

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Charged amino acids

Amino acids that have side chains that are charged either positively or negatively.

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Acidic amino acids

Amino acids that are negatively charged due to the presence of an additional carboxyl group.

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Examples of acidic amino acids

Aspartic acid, Glutamic acid.

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Basic amino acids

Amino acids that are positively charged due to the presence of amino groups.

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Examples of basic amino acids

Lysine, Arginine, Histidine.

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Proline

An amino acid where the side chain is connected to the main chain, creating a cyclic structure.

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Glycine

The most flexible amino acid due to its small side chain.

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Aliphatic side chains

Hydrophobic side chains that include alanine, valine, isoleucine, and leucine.

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Hydroxyl containing side chains

Side chains that contain -OH groups, such as serine and threonine.

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Negatively charged acidic residues

Aspartate and glutamate that have a negative charge.

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Basic side chains

The side chains of lysine and arginine that are positively charged.

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Cysteine

An amino acid that contains a sulfhydryl group and can form disulfide bonds with other cysteine residues.

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Disulfide bond

A covalent bond formed between two cysteine side chains, providing stability to proteins.

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Antibodies

Proteins that have a heavy chain with two disulfide bonds and a light chain connected by a disulfide bond.

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Alanine (A)

A nonpolar amino acid with a small side chain, unreactive.

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Arginine (R)

A positively charged amino acid that forms ionic interactions with negatively charged groups.

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Asparagine (N)

A polar, uncharged amino acid that can form hydrogen bonds.

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Aspartate (D)

A negatively charged amino acid that interacts with positively charged groups.

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Cysteine (C)

An amino acid with a reactive SH group that can form polar bonds.

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Glutamine (Q)

A polar, uncharged amino acid that can form hydrogen bonds.

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Glutamate (E)

A negatively charged amino acid commonly replacing aspartate.

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Histidine (H)

An amino acid that is partially charged around pH 7, contains a C3N2H4 ring.

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Isoleucine (I)

A hydrophobic, nonpolar amino acid commonly replacing valine.

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Leucine (L)

A hydrophobic, nonpolar, aliphatic amino acid.

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Lysine (K)

A positively charged, basic amino acid that forms ionic interactions.

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Methionine (M)

A nonpolar, hydrophobic amino acid that contains sulfur.

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Phenylalanine (F)

An aromatic, hydrophobic, nonreactive amino acid.

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Serine (S)

A polar, uncharged amino acid that contains a hydroxyl group.

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Threonine (T)

A polar, uncharged amino acid that also contains a hydroxyl group.

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Tryptophan (W)

A large, hydrophobic, aromatic amino acid reactive with nitrogen.

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Tyrosine (Y)

An aromatic amino acid that ionizes at pH 0 and is hydrophilic.

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Valine (V)

A hydrophobic, nonpolar amino acid that is aliphatic.

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Polar side chains

Side chains containing electronegative elements such as O, S, N.

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Acidic residues

Amino acids with negatively charged oxygen in their side chains.

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Basic residues

Amino acids with positively charged nitrogen in their side chains.