Acid induced equilibrium unfolding of annexin V wild type shows two intermediate states

被引：24

作者：

Beermann ofm cap, BB

Hinz, HJ

Hofmann, A

Huber, R

机构：

[1] Univ Munster, Inst Phys Chem, D-48149 Munster, Germany

[2] Max Planck Inst Biochem, Abt Strukturforsch, D-82152 Martinsried, Germany

来源：

FEBS LETTERS | 1998年 / 423卷 / 02期

关键词：

protein folding; intermediate; annexin V;

D O I：

10.1016/S0014-5793(98)00105-7

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：

Annexin V is an alpha-helical protein which shows anticoagulatory and antiinflammatory activity. It is supposed to be involved in membrane fusion and exocytosis. In this study acid-induced equilibrium unfolding of the human annexin V is investigated by fluorescence and circular dichroism spectroscopy. The spectroscopic data indicate that at least two intermediate states are involved in unfolding. One of the proposed intermediate states exhibits properties similar to those observed with annexin V wild type saturated with calcium, another map be regarded as 'molten globule'. (C) 1998 Federation of European Biochemical Societies.

引用

页码：265 / 269

页数：5

共 16 条

[1] STRUCTURAL AND ELECTROPHYSIOLOGICAL ANALYSIS OF ANNEXIN-V MUTANTS - MUTAGENESIS OF HUMAN ANNEXIN-V, AN IN-VITRO VOLTAGE-GATED CALCIUM-CHANNEL, PROVIDES INFORMATION ABOUT THE STRUCTURAL FEATURES OF THE ION PATHWAY, THE VOLTAGE SENSOR AND THE ION SELECTIVITY FILTER [J].