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Journal article

Dynamics, energetics, and selectivity of the low-K+ KcsA channel structure.

Abstract:

Potassium channels are a diverse family of integral membrane proteins through which K(+) can pass selectively. There is ongoing debate about the nature of conformational changes associated with the opening/closing and conductive/nonconductive states of potassium channels. The channels partly exert their function by varying their conductance through a mechanism known as C-type inactivation. Shortly after the activation of K(+) channels, their selectivity filter stops conducting ions at a rate ...

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Publication status:
Published

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Publisher copy:
10.1016/j.jmb.2009.04.038

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Journal:
Journal of molecular biology
Volume:
389
Issue:
3
Pages:
637-645
Publication date:
2009-06-05
DOI:
EISSN:
1089-8638
ISSN:
0022-2836
URN:
uuid:d8f96aab-5263-42ce-9669-5f2a5e7ac9e5
Source identifiers:
118290
Local pid:
pubs:118290

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