Characterization and modeling of membrane proteins using sequence analysis.
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.
Department of Medicine, University of Toronto, Canada.
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Reithmeier
D000595:Amino Acid Sequence; D003198:Computer Simulation; D006801:Humans; D008055:Lipids / Q000737:chemistry; D008565:Membrane Proteins / Q000737:chemistry*; D008969:Molecular Sequence Data; D011487:Protein Conformation; D017421:Sequence Analysis
D008055:Lipids; D008565:Membrane Proteins