Time-resolved small-angle neutron scattering of proteins in solution

被引：6
|
作者：
Rössle, M
Manakova, E
Holzinger, J
Vanatalu, K
May, RP
Heumann, H
机构：
[1] Max Planck Inst Biochem, D-82152 Martinsried, Germany
[2] Inst Max Von Laue Paul Langevin, F-38042 Grenoble, France
[3] Inst Chem Phys & Biophys, EE-0026 Tallinn, Estonia
来源：
PHYSICA B | 2000年 / 276卷
关键词：
biological structure; isotopic substitution; proteins; small-angle neutron scattering;
D O I：
10.1016/S0921-4526(99)01732-9
中图分类号：
O469 [凝聚态物理学];
学科分类号：
070205 ;
摘要：
Small-angle neutron solution scattering is a method used to obtain information about structural changes of proteins in solution. Time-resolved experiments were performed in the is time range at the ILL using the high flux small-angle scattering instrument D22. A stopped-flow apparatus was built for this purpose which permitted fast mixing of the reactants. The reaction of the GroE system with the nucleotide analog AMP-PNP was analysed under different contrast conditions using D-labelled proteins. Two conformational intermediate states of the chaperonin pathway were identified. (C) 2000 Elsevier Science B.V. All rights reserved.
引用
收藏
页码：532 / 533
页数：2
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