title: Ab initio protein folding.
abstract: Ab initio protein folding methods have been developing rapidly over the past few years and, at the last Critical assessment of methods of protein structure prediction (CASP) meeting, it was shown that important progress has been made in generating structure from sequence. Both methods based on statistical potentials and methods using physics-based potentials have shown improvements. Most current methods use statistics-based potentials and the development of these is ongoing. Additionally, the inclusion of multiple sequence data in the algorithms in order to aid in finding the native structure is a common theme. The use of physics-based potentials is less developed, which means that less progress has been made in understanding why a sequence forms a structure.
authors.affiliation: Department of Chemistry, University of Bath, Bath, BA2 7AY, UK. djosg@mgu.bath.ac.uk
authors.forename: D J
authors.initials: DJ
authors.lastname: Osguthorpe
mesh_terms: D000818:Animals; D003226:Congresses as Topic; D003626:Data Display; D006801:Humans; D008956:Models, Chemical; D011336:Probability; D011487:Protein Conformation; D017510:Protein Folding; D013816:Thermodynamics