Topology of Membrane Proteins

Gábor E. Tusnády and István Simon*
Institute of Enzymology, BRC, Hungarian Academy of Sciences, Budapest, Hungary, and Department of Biological Physics, Etvs Lornd University, Budapest, Hungary
J. Chem. Inf. Comput. Sci., 2001, 41 (2), pp 364–368
DOI: 10.1021/ci0001280
Publication Date (Web): February 14, 2001
Copyright © 2001 American Chemical Society
*

 To whom correspondence should be addressed:  Institute of Enzymology, BRC, Hungarian Academy of Sciences, P.O. Box 7, H-1518 Budapest, Hungary. Phone:  (36-1) 466-9276. Fax:  (36-1) 466-5465. E-mail: simon@enzim.hu.

Abstract

Integral membrane proteins play important roles in living cells. Due to difficulties of experimental techniques, theoretical approaches, i.e., topology prediction methods, are important for structure determination of this class of proteins. Here we show a detailed comparison of transmembrane topology prediction methods. According to this comparison, we conclude that the topology of integral membrane proteins is determined by the maximum divergence of the amino acid composition of sequence segments. These segments are located in different areas of the cell, which can be characterized by different physicochemical properties. The results of these prediction methods compared to the X-ray diffraction data of several transmembrane proteins will also be discussed.

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