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Titolo:
CRYSTAL-STRUCTURE OF A FLUORESCENT DERIVATIVE OF RNASE-A
Autore:
BAUDETNESSLER S; JULLIEN M; CROSIO MP; JANIN J;
Indirizzi:
UNIV PARIS 11,BIOL STRUCT LAB,CNRS,UMR 9920,BAT 433 F-91405 ORSAY FRANCE UNIV PARIS 11,BIOL STRUCT LAB,CNRS,UMR 9920,BAT 433 F-91405 ORSAY FRANCE
Titolo Testata:
Biochemistry
fascicolo: 33, volume: 32, anno: 1993,
pagine: 8457 - 8464
SICI:
0006-2960(1993)32:33<8457:COAFDO>2.0.ZU;2-2
Fonte:
ISI
Lingua:
ENG
Soggetto:
LEAST-SQUARES REFINEMENT; RIBONUCLEASE-A; SEMISYNTHETIC RIBONUCLEASE; MACROMOLECULAR STRUCTURES; ACTIVE-SITE; RESOLUTION; PRECRYSTALLIZATION; PACKING; BINDING; FORMS;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
31
Recensione:
Indirizzi per estratti:
Citazione:
S. Baudetnessler et al., "CRYSTAL-STRUCTURE OF A FLUORESCENT DERIVATIVE OF RNASE-A", Biochemistry, 32(33), 1993, pp. 8457-8464

Abstract

The crystal structure of RNase A chemically modified with the fluorescent probe, odoacetyl)-amino]ethyl]-5-naphthylamine-1-sulfonic (1,5-IAENS), has been solved and refined to high resolution. It yields information on the mode of binding, the mobility of a probe commonly used inspectroscopic studies, and anion binding sites in RNase A. Trigonal crystals of the fluorescent derivative grown in sodium or cesium chloride and ammonium sulfate, pH 5.1, were nearly isomorphous with those ofa semisynthetic RNase [DeMel, et al. (1992) J. Biol. Chem. 267, 247-256]. Refinement starting from semisynthetic RNase led to a model with R = 20% against 1.7-angstrom diffraction data from crystals in ammonium sulfate and another model with R = 17% against 1.9-angstrom data taken in the presence of 3 M NaCl. The second model contains three chloride ions: one is at the active site, and the other two are at molecularinterfaces. Otherwise, the two models are very similar. The fluorophore has very little effect on the protein conformation. It is found to be covalently attached to the active site His-12 with the naphthyl group stacked on the imidazole ring of His-119. It remains largely accessible to solvent and in a polar environment on the protein surface, even though the fluorescence emission spectrum is blue shifted as it is in nonpolar solvents.

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Documento generato il 28/11/20 alle ore 11:48:25