BOUND WATER AND STABILITY OF TRIPLE-HELICAL STRUCTURE OF COLLAGEN TYPE

被引：0
|
作者：
KHROMOVA, TB
LAZAREV, YA
机构：
来源：
BIOFIZIKA | 1986年 / 31卷 / 02期
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中图分类号：
Q6 [生物物理学];
学科分类号：
071011 ;
摘要：
The conformational transition triple-helix unordered chains of collagen-like polypeptide Z-(gly-pro-pro)8-OMe was studied by IR-, CD-spectroscopy and microcalorimetry. It was shown that the transition is .mchlt.all-or-none.mchgt. reaction. The obtained value of denaturation enthalpy per mole of tripeptide unit corresponds to hydration of one interpeptide H-bond in accordance with the Rich-Crick model. The contribution of bound water to enthalphy widely discussed for collagens was not revealed in synthetic polytripeptides.
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页码：208 / 212
页数：5
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