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Isopeptag Isopeptag is a 16 amino acid peptide tag that can be genetically linked to proteins without interfering with protein folding.〔(and Howarth,M. (2010). Spontaneous intermolecular amide bond formation between side chains for irreversible peptide targeting. J. Am. Chem. Soc. 132, 4526-4527. )〕 What makes the isopeptag different from other peptide tags is that it can bind its binding protein through a permanent and irreversible covalent bond. Other peptide tags generally bind their targets through weak non-covalent interactions, thus limiting their use in applications where molecules experience extreme forces. The isopeptags covalent binding to its target overcomes these barriers and allows target proteins to be studied in harsher molecular environments. == Development == The isopeptag was developed by dissecting the pilin protein (Spy0128) from ''Streptococcus pyogenes''. Spy0128 contains two intramolecular isopeptide bonds,〔Kang,H.J., Coulibaly,F., Clow,F., Proft,T., and Baker,E.N. (2007). Stabilizing isopeptide bonds revealed in gram-positive bacterial pilus structure. Science 318, 1625-1628.〕 and to generate the isopeptag one of these bonds was split by removing the last β-sheet in the protein.
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「Isopeptag」の詳細全文を読む
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