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Titolo:
WATER-MOLECULES IN DNA RECOGNITION I - HYDRATION LIFETIMES OF TRP OPERATOR DNA IN SOLUTION MEASURED BY NMR-SPECTROSCOPY
Autore:
SUNNERHAGEN M; DENISOV VP; VENU K; BONVIN AMJJ; CAREY J; HALLE B; OTTING G;
Indirizzi:
KAROLINSKA INST,DEPT MED BIOCHEM & BIOPHYS,DOKTORSRINGEN 9A1 S-17177 STOCKHOLM SWEDEN KAROLINSKA INST,DEPT MED BIOCHEM & BIOPHYS S-17177 STOCKHOLM SWEDEN LUND UNIV,DEPT CHEM,CONDENSED MATTER MAGNET RESONANCE GRP S-22100 LUND SWEDEN ETH ZENTRUM,PHYS CHEM LAB CH-8091 ZURICH SWITZERLAND PRINCETON UNIV,DEPT CHEM PRINCETON NJ 08544
Titolo Testata:
Journal of Molecular Biology
fascicolo: 4, volume: 282, anno: 1998,
pagine: 847 - 858
SICI:
0022-2836(1998)282:4<847:WIDRI->2.0.ZU;2-7
Fonte:
ISI
Lingua:
ENG
Soggetto:
PANCREATIC TRYPSIN-INHIBITOR; MINOR-GROOVE HYDRATION; AQUEOUS-SOLUTION; PROTEIN HYDRATION; BOUND WATER; RELAXATION; DODECAMER; DYNAMICS; SEQUENCE; BINDING;
Keywords:
TRP OPERATOR; DNA HYDRATION; NMR SPECTROSCOPY; PROTEIN/DNA RECOGNITION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
53
Recensione:
Indirizzi per estratti:
Citazione:
M. Sunnerhagen et al., "WATER-MOLECULES IN DNA RECOGNITION I - HYDRATION LIFETIMES OF TRP OPERATOR DNA IN SOLUTION MEASURED BY NMR-SPECTROSCOPY", Journal of Molecular Biology, 282(4), 1998, pp. 847-858

Abstract

The present NMR study investigates the residence times of the hydration water molecules associated with uncomplexed frp operator DNA in solution by measuring intermolecular nuclear Overhauser effects (NOE) between water and DNA protons, and the nuclear magnetic relaxation dispersion (NMRD) of the water H-2 and O-17 resonances. Both methods indicate that the hydration water molecules exchange with bulk water on the sub-nanosecond time scale at 4 degrees C. No evidence was obtained for water molecules bound with longer residence times. In particular, the water molecules at the sites of interfacial hydration in the trp repressor/operator complex do not seem kinetically stabilized in the uncomplexed DNA. Analysis of the crystal structures of two different frp repressor/operator complexes shows very similar structural environments for the water molecules mediating specific contacts between the proteinand the DNA, whereas much larger variations are observed for the location of corresponding water molecules detected in the crystal structure of an uncomplexed frp operator DNA duplex. Therefore, it appears unlikely that the hydration characteristics of the uncomplexed DNA targetwould be a major determinant of trp repressor/operator recognition. (C) 1998 Academic Press.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 20/09/20 alle ore 07:46:47