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PMID: 11277724 Published · ppublish English Comparative Study Journal Article Research Support, Non-U.S. Gov't

Topology of membrane proteins.

Journal of chemical information and computer sciences ·Vol. 41 ·No. 2 ·2001-00-00 ·Pages 364-8

Tusnády GE, Simon I

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.

MeSH Terms
Algorithms Amino Acids/analysis Chemical Phenomena Chemistry, Physical Membrane Proteins/chemistry Protein Structure, Secondary X-Ray Diffraction
Chemicals
Amino Acids Membrane Proteins
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Tusnády G E
Institute of Enzymology, BRC, Hungarian Academy of Sciences, Budapest, Hungary.
Simon I
Article Info
Journal
Journal of chemical information and computer sciences
Abbr.
J Chem Inf Comput Sci
ISSN
0095-2338
Published
2001-00-00
Pages
364-8
Language
English
Region
United States
NLM ID
7505012
Subset
IM
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