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Journal article

Conformational changes during the gating of a potassium channel revealed by structural mass spectrometry.

Abstract:

Potassium channels are dynamic proteins that undergo large conformational changes to regulate the flow of K(+) ions across the cell membrane. Understanding the gating mechanism of these channels therefore requires methods for probing channel structure in both their open and closed conformations. Radiolytic footprinting is used to study the gating mechanism of the inwardly-rectifying potassium channel KirBac3.1. The purified protein stabilized in either open or closed conformations was exposed...

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Publication status:
Published

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Publisher copy:
10.1016/j.str.2010.04.012

Authors


More by this author
Institution:
University of Oxford
Division:
MPLS
Department:
Physics
Role:
Author
More by this author
Institution:
University of Oxford
Division:
MPLS
Department:
Physics
Sub department:
Condensed Matter Physics
Role:
Author
Journal:
Structure (London, England : 1993)
Volume:
18
Issue:
7
Pages:
839-846
Publication date:
2010-07-01
DOI:
EISSN:
1878-4186
ISSN:
0969-2126
Language:
English
Keywords:
Pubs id:
pubs:66160
UUID:
uuid:6a9dc82e-237e-430d-88b6-093c53842492
Local pid:
pubs:66160
Source identifiers:
66160
Deposit date:
2012-12-19

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