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Titolo:
MOLECULAR-DYNAMICS SIMULATION OF INTERACTION OF HISTONE-LIKE PROTEIN OF MYCOBACTERIUM-TUBERCULOSIS (HLPMT) AND HISTONE OF CLOSTRIDIUM-PASTEURIANUM (DBHCLOPA) WITH 35-BASED PAIRED GC RICH U-BEND DNA
Autore:
KOTHEKAR V; RAHA K; PRASAD HJ;
Indirizzi:
ALL INDIA INST MED SCI,DEPT BIOPHYS NEW DELHI 110029 INDIA ALL INDIA INST MED SCI,DEPT BIOTECHNOL NEW DELHI 110029 INDIA
Titolo Testata:
Journal of biomolecular structure & dynamics
fascicolo: 2, volume: 16, anno: 1998,
pagine: 223 - 235
SICI:
0739-1102(1998)16:2<223:MSOIOH>2.0.ZU;2-#
Fonte:
ISI
Lingua:
ENG
Soggetto:
SECONDARY STRUCTURE PREDICTION; NUCLEIC-ACIDS; FORCE-FIELD; CONFORMATION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
31
Recensione:
Indirizzi per estratti:
Citazione:
V. Kothekar et al., "MOLECULAR-DYNAMICS SIMULATION OF INTERACTION OF HISTONE-LIKE PROTEIN OF MYCOBACTERIUM-TUBERCULOSIS (HLPMT) AND HISTONE OF CLOSTRIDIUM-PASTEURIANUM (DBHCLOPA) WITH 35-BASED PAIRED GC RICH U-BEND DNA", Journal of biomolecular structure & dynamics, 16(2), 1998, pp. 223-235

Abstract

Three dimensional structure of the first ninety two residues of histone like protein from Mycobacterium tuberculosis (Hlpmt) and histone ofClostridium pasteurianum (DBHclopa) are obtained here, on the basis of amino acid sequences of the two proteins, making use of secondary structure prediction programs, sequence search and HOMOLOGY based modeling tools available on Internet. The proteins were docked to a 35 base paired GC rich U bend DNA (U35DNA). Structures of proteins Hlpmt and DBHclopa; U35DNA; and complexes: Hlpmt-U35DNA and DBHclopa-U35DNA were optimized by molecular mechanics (MM) and simulated for 260 pico seconds (ps) in vacuum by molecular dynamics (MD) technique using AMBER 4.0package with Cornell et at force field. The proteins, when simulated alone, showed compaction. DBHclopa showed larger compaction compared with Hlpmt. U35DNA when simulated alone straightened out and assumed a B-form. In the complexes, Hlpmt showed same order of compaction as in absence of DNA, while DBHclopa showed reduced compaction. In the presence of Hlpmt two ends of helicoidal axis of U35DNA came closer, but slightly out of plane, indicative of its role in overwinding and packaging double stranded DNA. DBHclopa did not give rise to DNA overwinding. The results show architectural role of Hlpmt and DBHclopa in DNA packaging and its sequence dependence.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 30/09/20 alle ore 04:41:45