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PMID: 8528765 Published · ppublish English Journal Article Review

Characterization and modeling of membrane proteins using sequence analysis.

Current opinion in structural biology ·Vol. 5 ·No. 4 ·1995-08-00 ·Pages 491-500

Reithmeier RA

Abstract

The current libraries of amino acid sequences of membrane proteins are a valuable resource for the analysis of elements common to these proteins. Multiple-sequence alignment techniques and the identification of conserved features of transmembrane segments have improved the prediction of membrane protein topology. Molecular modeling in combination with structural studies or site-directed mutagenesis is proving to be a powerful link between theory and experiment. Unfortunately, the number of high-resolution structures of intrinsic membrane proteins, although increased recently, presents a restricted and perhaps biased view of membrane protein structure.

MeSH Terms
Amino Acid Sequence Computer Simulation Humans Lipids/chemistry Membrane Proteins/chemistry Molecular Sequence Data Protein Conformation Sequence Analysis
Chemicals
Lipids Membrane Proteins
Authors & Affiliations
1 authors, click to expand affiliations / ORCID
Reithmeier R A
Department of Medicine, University of Toronto, Canada.
Article Info
Journal
Current opinion in structural biology
Abbr.
Curr Opin Struct Biol
ISSN
0959-440X
Published
1995-08-00
Pages
491-500
Language
English
Region
England
NLM ID
9107784
Subset
IM
Analysis Services
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