Literature DB >> 11277724

Topology of membrane proteins.

G E Tusnády1, I Simon.   

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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Year:  2001        PMID: 11277724     DOI: 10.1021/ci0001280

Source DB:  PubMed          Journal:  J Chem Inf Comput Sci        ISSN: 0095-2338


  11 in total

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2.  Deuterium/hydrogen exchange factors measured by solution nuclear magnetic resonance spectroscopy as indicators of the structure and topology of membrane proteins.

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6.  Comparative analyses of transport proteins encoded within the genomes of Leptospira species.

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8.  Comparative genomic analyses of transport proteins encoded within the genomes of Leptospira species.

Authors:  Bora Buyuktimkin; Milton H Saier
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9.  PDB_TM: selection and membrane localization of transmembrane proteins in the protein data bank.

Authors:  Gábor E Tusnády; Zsuzsanna Dosztányi; István Simon
Journal:  Nucleic Acids Res       Date:  2005-01-01       Impact factor: 16.971

10.  A simple method for predicting transmembrane proteins based on wavelet transform.

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