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Domain
From Proteopedia
A protein domain is a sequence of amino acids that folds, independently of the remainder of the full-length sequence, into a compact stable structure. Water-soluble domains typically have hydrophobic cores. Some small full-length proteins consist of a single domain, but most proteins have two or more domains. A domain is typically 100-250 amino acids in length[1], but can sometimes be shorter or longer.
Examples:
- 9ins: Insulin, with 51 amino acids, is one of the smallest stably folded protein domains, on the boundary between a protein and a peptide. It has a hydrophobic core. Preproinsulin is synthesized as 108 amino acids. After removal of a 24 amino acid signal sequence, the remaining 84 amino acid proinsulin is cleaved in two places, forming a disulfide-linked dimer of two protein chains of 21 and 30 residues (total: 51).
- 2hhd: Each of the 4 chains that form hemoglobin (a tetramer) folds into a single domain composed of alpha-helices. Each domain (chain) is 141-146 amino acids in length for human hemoglobin.
- 1igy: Immunoglobulin G (antibody) consists of 12 domains in 4 chains. These domains are composed of beta-sheets. Each of the two heavy chains has 4 domains, and each of the 2 light chains has 2 domains. These domains are about 110 amino acids in length. Each heavy chain has two pairs of domains connected by a flexible linker about 20 amino acids in length.
For more information see Protein Domain in Wikipedia.
See also [1] and this summary of it.
