title: De novo membrane protein structure prediction.
abstract: Recent advances in identifying residue-residue contacts from large multiple sequence alignments have enabled impressive gains to be made in the field of protein structure prediction. In this chapter, we discuss these advances and provide a step-by-step guide to applying the latest tools to the de novo modelling of alpha-helical transmembrane proteins. As a practical example, we demonstrate the process of building an accurate 3D model of a G protein-coupled receptor, correctly orientated in the membrane, using only its primary protein sequence.
authors.affiliation: Bioinformatics Group, Department of Computer Science, University College London, Office: 8.11, Desk: 206, Gower Street, London, WC1E 6BT, UK, t.nugent@cs.ucl.ac.uk.
authors.forename: Timothy
authors.initials: T
authors.lastname: Nugent
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D002417:Cattle; D019295:Computational Biology / Q000379:methods*; D008565:Membrane Proteins / Q000737:chemistry*; D008958:Models, Molecular; D008969:Molecular Sequence Data; D017433:Protein Structure, Secondary; D012243:Rhodopsin / Q000737:chemistry; D013696:Temperature
chemical_list: D008565:Membrane Proteins; D012243:Rhodopsin