Reithmeier R A
Department of Medicine, University of Toronto, Canada.
Curr Opin Struct Biol. 1995 Aug;5(4):491-500. doi: 10.1016/0959-440x(95)80034-4.
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.
