title: Ab initio folding of multiple-chain proteins.
abstract: Our previous methodology for ab initio prediction of protein structure is extended here to treat multiple-chain proteins. This involved modification of our united-residue (UNRES) force field and our Conformational Space Annealing (CSA) Global Optimization procedure. Good results have been obtained for both a four- and a three-helix protein from the CASP3 exercise.
authors.affiliation: Baker Laboratory of Chemistry and Chemical Biology, Cornell University, Ithaca, NY 14853-1301, USA.
authors.forename: J A
authors.initials: JA
authors.lastname: Saunders
authors.forename: K D
authors.initials: KD
authors.lastname: Gibson
authors.forename: H A
authors.initials: HA
authors.lastname: Scheraga
mesh_terms: D019281:Dimerization; D004220:Disulfides / Q000737:chemistry; D046911:Macromolecular Substances; D008958:Models, Molecular; D011487:Protein Conformation; D017510:Protein Folding; D021122:Protein Subunits; D011506:Proteins / Q000737:chemistry / Q000378:metabolism*; D013816:Thermodynamics
chemical_list: D004220:Disulfides; D046911:Macromolecular Substances; D021122:Protein Subunits; D011506:Proteins