Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
1944529 | Biochimica et Biophysica Acta (BBA) - Biomembranes | 2012 | 7 Pages |
Abstract
⺠Solid-state 31P MAS NMR studies have been used to characterise binding to the non-annular binding site of KcsA. ⺠Residues R64 and R89 have been identified as important in the recognition of anionic lipids in the non-annular binding site. ⺠Single-channel current recordings demonstrate the functional importance of these interactions for KcsA activity.
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Authors
Phedra Marius, Maurits R.R. de Planque, Philip T.F. Williamson,