Secondary structure, stability and tetramerisation of recombinant Kv1.1 potassium channel cytoplasmic N-terminal fragment.

G.W. Abbott, M. Bloemendal, I.H.M. van Stokkum, E.A.J. Mercer, R.T. Miller, S. Sewing, M.J.J. Wolters, O. Pongs, S.K.S. Srai

Research output: Contribution to JournalArticleAcademicpeer-review

Abstract

The recombinant N-terminal fragment (amino acids 14-162) of a tetrameric voltage-gated potassium channel (K(V)1.1) has been studied using spectroscopic techniques. Evidence is presented that it forms a tetramer in aqueous solution, whereas when solubilised in 1% Triton X-100 it remains monomeric. The secondary structure content of both monomeric and tetrameric K,1.1 N-terminal fragment has been estimated from FTIR and CD spectroscopy to be 20-25% a-helix, 20-25% β-sheet, 20% turns and 30-40% random coil. Solubilisation of the protein in detergent is shown by hydrogen-deuterium exchange analysis to alter tertiary structure rather than secondary structure and this may be the determining factor in tetramerisation ability. Using molecular modelling we propose a super secondary structure consisting of two structural domains.
Original languageEnglish
Pages (from-to)71-78
JournalBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology
Volume1341
DOIs
Publication statusPublished - 1997

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