References--Dr. Paul J. Pfaffinger's Lab
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Molecular Biology and Biophysics of Potassium Ion Channels
Div. of Neuroscience
Baylor College of Medicine
Houston, Texas, USA

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Baylor College of Medicine

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EndNote#: 537 Reference Type: Journal Article


Author:

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


Year:

1997


Article/
Book Sect.:

Secondary structure, stability and tetramerisation of recombinant K(V)1.1 potassium channel cytoplasmic N-terminal fragment


Journal/
Book:

Biochimica et Biophysica Acta


Volume:

1341

Number:

1
Pages: 71-8 Label:




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(V)1.1 N-terminal fragment has been estimated from FTIR and CD spectroscopy to be 20-25% alpha-helix, 20-25% beta-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 supersecondary structure consisting of two structural domains.

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