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I222 crystal form of despentapeptide (B26-B30) insulin provides new insights into the properties of monomeric insulin
- 1.0048758 - ÚOCHB 2007 RIV DK eng J - Journal Article
Whittingham, J. L. - Youshang, Z. - Žáková, Lenka - Dodson, E. J. - Turkenburg, J. P. - Brange, J. - Dodson, G. G.
I222 crystal form of despentapeptide (B26-B30) insulin provides new insights into the properties of monomeric insulin.
[I222 krystalová forma despentapeptid (B26-B30) insulinu podává nové informace o vlastnostech monomerního insulinu.]
Acta Crystallographica Section D-Biological Crystallography. Roč. 62, č. 5 (2006), s. 505-511. ISSN 0907-4449
Institutional research plan: CEZ:AV0Z40550506
Keywords : insulin * crystal structure * monomer * despentapeptid
Subject RIV: CE - Biochemistry
Impact factor: 1.687, year: 2006
Despentapeptide (des-B26-B30)insulin has been crystallized and the crystal structure analysis revealed that this molecule is unable to make beta-strand interactions for physiological dimer formation and is apparently monomeric in solution.
Despentapeptid (des-B26-B30)insulin byl krystalizován a analýza krystalové struktury ozřejmila že tato molekula není schopná vytvářet interakce mezi beta-strukturami, které jsou nezbytné pro formování dimerů. Despentapeptid (des-B26-B30)insulin je proto s velkou pravděpodobností v roztoku monomerní.
Permanent Link: http://hdl.handle.net/11104/0003778
Number of the records: 1