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A protein ''domain'' is a sequence of amino acids that can fold, 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<ref name="EPR" />, but can sometimes be shorter or longer. | A protein ''domain'' is a sequence of amino acids that can fold, 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<ref name="EPR" />, but can sometimes be shorter or longer. | ||
Examples: | |||
* Each of the 4 chains that form hemoglobin (a tetramer) folds into a single domain. See [[2hhd]]. | |||
For more information see [http://www.wikipedia.com/wiki/Protein_domain Protein Domain in Wikipedia]. | For more information see [http://www.wikipedia.com/wiki/Protein_domain Protein Domain in Wikipedia]. | ||
Revision as of 23:55, 14 February 2016
A protein domain is a sequence of amino acids that can fold, 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:
- Each of the 4 chains that form hemoglobin (a tetramer) folds into a single domain. See 2hhd.
For more information see Protein Domain in Wikipedia.
See also [1] and this summary of it.