Issues
1 March 2009
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Cover Image
Cover Image
Cover picture: Accessibility to trypsin digestion of BK channel β-subunit N termini reveals their sequestration in the channel antechamber. (Top) Schematic of the pathway for access of the β2 N-terminal inactivation domain to the BK channel central cavity. (Bottom) Model of the hypothesis that N termini transiently bind in the antechamber between the pore and cytosolic domains, resulting in reduced rates of trypsin digestion even in closed channels (see article by Zhang et al., 263–282).
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ISSN 0022-1295
EISSN 1540-7748
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Voltage-Gated Na Channels
Drugs exhibit diverse binding modes and access routes in the Nav1.5 cardiac sodium channel pore
Mechanotransduction by Membrane Proteins
Mechanosensitive channel MscS is critical for termination of the bacterial hypoosmotic permeability response
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