Domain: Difference between revisions
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Examples: | 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. | * [[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. | * [[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. | ||