Ion mobility-mass spectrometry reveals long-lived, unfolded intermediates in the dissociation of protein complexes

被引：188
|
作者：
Ruotolo, Brandon T.
Hyung, Suk-Joon
Robinson, Paula M.
Giles, Kevin
Bateman, Robert H.
Robinson, Carol V.
机构：
[1] Univ Cambridge, Dept Chem, Cambridge CB2 1EW, England
[2] Waters MS Technol Ctr, Manchester M23 9LZ, Lancs, England
来源：
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION | 2007年 / 46卷 / 42期
关键词：
dissociation; electrospray ionization; mass spectrometry; protein structures;
D O I：
10.1002/anie.200702161
中图分类号：
O6 [化学];
学科分类号：
0703 ;
摘要：
Folded or not? Ion mobility-mass spectrometry investigation of an activated macromolecular protein complex lends insight into the structures of intermediates formed in the dissociation process. The activated ions of human tetrameric transthyretin populate partially folded intermediate states (see picture; folded subunits in blue, partially unfolded subunits in red) prior to dissociation. (Figure Presented). © 2007 Wiley-VCH Verlag GmbH & Co. KGaA.
引用
收藏
页码：8001 / 8004
页数：4
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