Substitution of a hydrophobic residue alters the conformational stability of Shaker K+ channels during gating and assembly.

A leucine residue at position 370 (L370) in 29-4 Shaker K+ channels resides within two overlapping sequence motifs conserved among most voltage-gated channels: the S4 segment and a leucine heptad repeat. Here we investigate the effects observed upon substitution of L370 with many other uncharged ami...

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Bibliographic Details
Main Authors: McCormack, K, Lin, L, Sigworth, F J
Format: Artigo
Language:Inglês
Published: 1993
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Research Article
Online Access:https://ncbi.nlm.nih.gov/pmc/articles/PMC1225901/
https://ncbi.nlm.nih.gov/pubmed/8274662
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