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Haemadin
In molecular biology, haemadin is an anticoagulant peptide synthesised by the Indian leech, ''Haemadipsa sylvestris''. It adopts a secondary structure consisting of five short beta-strands (beta1-beta5), which are arranged in two antiparallel distorted sheets formed by strands beta1-beta4-beta5 and beta2-beta3 facing each other. This beta-sandwich is stabilised by six enclosed cysteines arranged in a (3-5, 4-6 ) disulfide pairing resulting in a disulfide-rich hydrophobic core that is largely inaccessible to bulk solvent. The close proximity of disulfide bonds () and () organises haemadin into four distinct loops. The N-terminal segment of this domain binds to the active site of thrombin, inhibiting it. ==References==
抄文引用元・出典: フリー百科事典『 ウィキペディア(Wikipedia)』 ■ウィキペディアで「Haemadin」の詳細全文を読む
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