UV-visible derivative spectroscopy under high pressure

被引：117

作者：

Lange, R ^{[1
]}

Balny, C ^{[1
]}

机构：

[1] CNRS, INSERM, U128, IFR 24, F-34293 Montpellier 5, France

来源：

BIOCHIMICA ET BIOPHYSICA ACTA-PROTEIN STRUCTURE AND MOLECULAR ENZYMOLOGY | 2002年 / 1595卷 / 1-2期

关键词：

high pressure; absorbance spectroscopy; derivative; protein inactivation; folding; unfolding;

D O I：

10.1016/S0167-4838(01)00336-3

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：

High hydrostatic pressure affects proteins, changing their intra- or intermolecular interactions, conformation and solvation. How to detect these changes? In this paper, via some selected examples, we show the potentiality (but also the limits) of the ultraviolet derivative spectroscopy specially adapted to high pressure experiments. (C) 2002 Elsevier Science B.V. All rights reserved.

引用

页码：80 / 93

页数：14

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