A PATHWAY FOR THE THERMAL DESTABILIZATION OF BACTERIORHODOPSIN

被引：46

作者：

TANEVA, SG

CAAVEIRO, JMM

MUGA, A

GONI, FM

机构：

[1] UNIV BASQUE COUNTRY,DEPT BIOCHEM,E-48080 BILBAO,SPAIN

[2] ACAD G BONCHEV,CENT LAB BIOPHYS,BU-1113 SOFIA,BULGARIA

来源：

FEBS LETTERS | 1995年 / 367卷 / 03期

关键词：

PROTEIN DENATURATION; PROTEIN UNFOLDING; INFRARED SPECTROSCOPY; COMPACT DENATURED STATE; BACTERIORHODOPSIN;

D O I：

10.1016/0014-5793(95)00570-Y

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：

A variety of structural techniques, including IR spectroscopy, reveals that thermal denaturation of bacteriorhodopsin follows a given pathway (successively rearrangement of helical structures, extensive deuterium exchange, and finally protein aggregation) irrespective of heating rate, pH or ionic strength conditions, In all cases, thermal denaturation leads to a 'compact denatured state' which retains a large proportion of ordered structure.

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页码：297 / 300

页数：4

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