Temperature- and pressure-induced unfolding of α-chymotrypsin

被引：0

作者：

Sun, Z ^{[1
]}

Winter, R ^{[1
]}

机构：

[1] Univ Dortmund, Dept Chem, D-44227 Dortmund, Germany

来源：

ADVANCES IN HIGH PRESSURE BIOSCIENCE AND BIOTECHNOLOGY II, PROCEEDINGS | 2003年

关键词：

D O I：

暂无

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The temperature and pressure dependence on the secondary structure of alpha-chymotrypsin was studied by FT-IR spectroscopy. The temperature dependence of the secondary structures of alpha-chymotrypsin indicates that the temperature-induced unfolding of alpha-chymotrypsin sets in at 41degreesC and pD 7.0 at ambient pressure. Upon unfolding, the content of intermolecular beta-sheet structures increases drastically, whereas that of intramolecular beta-sheets decrease concomitantly. At room temperature (21 degreesC), this protein denatures at similar to4.9 kbar. No aggregation occurs in the pressure-denaturated state. A tentative p-T stability diagram was obtained on the basis of pressure dependent FT-IR measurements at different temperatures.

引用

页码：117 / 120

页数：4

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