Towards genome-scale structure prediction for transmembrane proteins

Philos Trans R Soc Lond B Biol Sci. 2006 Mar 29;361(1467):465-75. doi: 10.1098/rstb.2005.1804.


In this paper we briefly review some of the recent progress made by ourselves and others in developing methods for predicting the structures of transmembrane proteins from amino acid sequence. Transmembrane proteins are an important class of proteins involved in many diverse biological functions, many of which have great impact in terms of disease mechanism and drug discovery. Despite their biological importance, it has proven very difficult to solve the structures of these proteins by experimental techniques, and so there is a great deal of pressure to develop effective methods for predicting their structure. The methods we discuss range from methods for transmembrane topology prediction to new methods for low resolution folding simulations in a knowledge-based force field. This potential is designed to reproduce the properties of the lipid bilayer. Our eventual aim is to apply these methods in tandem so that useful three-dimensional models can be built for a large fraction of the transmembrane protein domains in whole proteomes.

Publication types

  • Review

MeSH terms

  • Cell Membrane / chemistry
  • Cell Membrane / metabolism*
  • Computational Biology
  • Genome*
  • Membrane Proteins / chemistry*
  • Membrane Proteins / classification
  • Membrane Proteins / genetics*
  • Membrane Proteins / metabolism
  • Models, Molecular
  • Protein Folding


  • Membrane Proteins