Hostname: page-component-586b7cd67f-rdxmf Total loading time: 0 Render date: 2024-11-30T23:29:25.445Z Has data issue: false hasContentIssue false
  • English
  • Français

A Phenomenological Model of the LS2 Ion Channel

Published online by Cambridge University Press:  15 February 2011

Qingfeng Zhong ,
Dennis M. Newns  and
Michael L. Klein
Qingfeng Zhong
Affiliation:
Center for Molecular Modeling and Department of Chemistry, University of Pennsylvania, Philadelphia, PA 19104-6323
Dennis M. Newns
Affiliation:
Thomas J. Watson Research Center, International Business Machines Corporation, Yorktown Heights, NY 10598
Michael L. Klein
Affiliation:
Center for Molecular Modeling and Department of Chemistry, University of Pennsylvania, Philadelphia, PA 19104-6323
Get access

Abstract

A molecular dynamics simulation has been performed on a synthetic membrane-spanning ion channel, consisting of four α-helical peptides, each of which is composed of the sequence Ac-(LSLLLSL)3-CONH2. In the present simulation, the channel was initially assembled dynamically as a parallel bundle in the octane portion of a phase separated water/octane system, which provided a membrane-mimetic environment, without imposing any structural constraints. After more than one nanosecond, the four helices were found to adopt an associated dimer state with two-fold symmetry, which after a further 3 ns evolved to a coiled-coil tetrameric structure with a left-handed twist. Based on the simulation, we proposed a phenomenological model to describe the two-states of the channel.

Keywords

Ion channelfour-helix bundlemolecular dynamicssynthetic proton channela-helical peptide
Type
Research Article
Information
MRS Online Proceedings Library (OPL) , Volume 489: Symposium K – Materials Science of the Cell , 1997 , 131
Copyright
Copyright © Materials Research Society 1998

Access options

Get access to the full version of this content by using one of the access options below. (Log in options will check for institutional or personal access. Content may require purchase if you do not have access.)

References

[1] Lear, J.D., Wasserman, Z.R., and DeGrado, W.F., Science 240, 1177–1181 (1988).Google Scholar
[2] Woolf, T.B., and Roux, B., Proc. Natl. Acad. Sci. USA. 91, 11631–11635 (1994).Google Scholar
[3] Elber, R., Chen, D.P., Rojewska, D., and Eisenberg, R., Biophys. J. 68, 906–924 (1995).Google Scholar
[4] Pullman, A., Chem. Rev. 91, 793–812 (1991).Google Scholar
[5] Sansom, M.S.P.. Sankararamakrishnan, H.S.S.R., Kerr, I.D., and Breed, J., Biophys. J. 68, 1295–1310 (1995).Google Scholar
[6] Martyna, G.J., Tuckerman, M., Tobias, D.J., and Klein, M.L., Mol. Phys. 87, 1117–1157 (1996).Google Scholar
[7] Jorgensen, W.L., Chandresekhar, J., Madura, J.D., Impey, R.W., and Klein, M.L., J. Chem. Phys. 79, 926–935 (1983).Google Scholar
[8] Tuckerman, M.. Berne, B.J.. and Martyna, G.J., J. Chem. Phys. 97, 1990–2001 (1992).Google Scholar
[9] Siepmann, J.I.. Karaborni, S., and Smit, B., Nature 365, 330–332 (1993).Google Scholar
[10] Brooks, B.R., Bruccoleri, R.E., Olafson, B.D., States, D.J., Swaminathan, S., and Karplus, M., J. Comp. Chem. 4, 187–217 (1983).Google Scholar
[11] Zhong, Q.F., Jiang, Q., Moore, P.B., Newns, D.M., and Klein, M.L., to be appeared in Biophys. J. 74, (1998).Google Scholar