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Solution-based single-molecule FRET studies of K(+) channel gating in a lipid bilayer..

Abstract:

Ion channels are dynamic multimeric proteins that often undergo multiple unsynchronized structural movements as they switch between their open and closed states. Such structural changes are difficult to measure within the context of a native lipid bilayer and have often been monitored via macroscopic changes in Förster resonance energy transfer (FRET) between probes attached to different parts of the protein. However, the resolution of this approach is limited by ensemble averaging of structu...

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Publication status:
Published
Peer review status:
Peer reviewed
Version:
Publisher's version

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Publisher copy:
10.1016/j.bpj.2016.05.020

Authors


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Institution:
University of Oxford
Division:
MPLS Division
Department:
Physics
Role:
Author
More by this author
Institution:
University of Oxford
Division:
MPLS Division
Department:
Physics; Condensed Matter Physics
Oxford college:
St Cross College
Role:
Author
More by this author
Institution:
University of Oxford
Division:
MPLS Division
Department:
Physics; Condensed Matter Physics
Oxford college:
Green Templeton College
Role:
Author
ORCID:
0000-0001-8996-2000
Engineering and Physical Sciences Research Council More from this funder
Wellcome Trust More from this funder
European Union More from this funder
Publisher:
Elsevier Publisher's website
Journal:
Biophysical Journal Journal website
Volume:
110
Issue:
12
Pages:
2663-2670
Publication date:
2016-06-05
Acceptance date:
2016-05-09
DOI:
EISSN:
1542-0086
ISSN:
0006-3495
Pubs id:
pubs:631031
URN:
uri:03bf9ca6-7e6e-4cae-9f32-99d84996e431
UUID:
uuid:03bf9ca6-7e6e-4cae-9f32-99d84996e431
Local pid:
pubs:631031

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