Ab initio folding of multiple-chain proteins.
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.
Saunders
J A
JA
Baker Laboratory of Chemistry and Chemical Biology, Cornell University, Ithaca, NY 14853-1301, USA.
Gibson
K D
KD
Scheraga
H A
HA
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
D004220:Disulfides; D046911:Macromolecular Substances; D021122:Protein Subunits; D011506:Proteins