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Titolo:
Calculation of protein conformation by global optimization of a potential energy function
Autore:
Lee, J; Liwo, A; Ripoll, DR; Pillardy, J; Scheraga, HA;
Indirizzi:
Cornell Univ, Baker Lab Chem & Chem Biol, Ithaca, NY 14853 USA Cornell Univ Ithaca NY USA 14853 b Chem & Chem Biol, Ithaca, NY 14853 USA Univ Gdansk, Fac Chem, PL-80952 Gdansk, Poland Univ Gdansk Gdansk PolandPL-80952 sk, Fac Chem, PL-80952 Gdansk, Poland Cornell Univ, Ctr Theory, Ithaca, NY 14853 USA Cornell Univ Ithaca NY USA14853 l Univ, Ctr Theory, Ithaca, NY 14853 USA
Titolo Testata:
PROTEINS-STRUCTURE FUNCTION AND GENETICS
, , anno: 1999, supplemento:, 3
pagine: 204 - 208
SICI:
0887-3585(1999):<204:COPCBG>2.0.ZU;2-N
Fonte:
ISI
Lingua:
ENG
Soggetto:
RESIDUE FORCE-FIELD; MEMBRANE-BOUND PORTION; STRUCTURE SIMULATIONS; POLYPEPTIDES; PREDICTION; PARAMETERS; MELITTIN;
Keywords:
protein folding; global optimization; conformational search; potential energy function; structure prediction;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
20
Recensione:
Indirizzi per estratti:
Indirizzo: Scheraga, HA Cornell Univ, Baker Lab Chem & Chem Biol, Ithaca, NY 14853 USA Cornell Univ Ithaca NY USA 14853 Biol, Ithaca, NY 14853 USA
Citazione:
J. Lee et al., "Calculation of protein conformation by global optimization of a potential energy function", PROTEINS, 1999, pp. 204-208

Abstract

A novel hierarchical approach to protein folding has been applied to compute the unknown structures of seven target proteins provided by CASP3. The approach is based exclusively on the global optimization of a potential energy function for a united-residue model by conformational space annealing, followed by energy refinement using an all-atom potential. Comparison of thesubmitted models for five globular proteins with the experimental structures shows that the conformations of large fragments (similar to 60 aa) were predicted with rmsds of 4.2-6.8 Angstrom for the C-alpha atoms. Our lowest-energy models for targets T0056 and T0061 were particularly successful, producing the correct fold of approximately 52% and 80% of the structures, respectively These results support the thermodynamic hypothesis that protein structure can be computed solely by global optimization of a potential energy function for a given amino acid sequence. (C) 1999 Wiley-Liss, Inc.

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Documento generato il 02/07/20 alle ore 22:15:40