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Titolo:
Protein interactions in concentrated ribonuclease solutions
Autore:
Boyer, M; Roy, MO; Jullien, M; Bonnete, F; Tardieu, A;
Indirizzi:
Univ14,ntpellier 1, Fac Pharm, Ctr Biochim Struct, CNRS UMR C9955,INSERM U4 Univ Montpellier 1 Montpellier France F-34060 , CNRS UMR C9955,INSERM U4 Univ Paris 06, Lab Mineral Cristallog, CNRS UMR 7590, Paris 05, France Univ Paris 06 Paris France 05 ristallog, CNRS UMR 7590, Paris 05, France Univ Paris 07, Lab Mineral Cristallog, CNRS UMR 7590, Paris 05, France Univ Paris 07 Paris France 05 ristallog, CNRS UMR 7590, Paris 05, France
Titolo Testata:
JOURNAL OF CRYSTAL GROWTH
fascicolo: 2-4, volume: 196, anno: 1999,
pagine: 185 - 192
SICI:
0022-0248(199901)196:2-4<185:PIICRS>2.0.ZU;2-Z
Fonte:
ISI
Lingua:
ENG
Soggetto:
PHOTON-CORRELATION SPECTROSCOPY; X-RAY-SCATTERING; LIGHT-SCATTERING; CRYSTAL-GROWTH; PRECRYSTALLIZATION; RESOLUTION; REFINEMENT;
Keywords:
protein interactions; crystallization; ribonuclease A; dynamic light scattering; small angle X-ray scattering;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Physical, Chemical & Earth Sciences
--discip_EC--
Citazioni:
27
Recensione:
Indirizzi per estratti:
Indirizzo: Jullien, M Univ14,ntpellier 1, Fac Pharm, Ctr Biochim Struct, CNRS UMR C9955,INSERM U4 Univ Montpellier 1 15 Ave Charles Flahault Montpellier FranceF-34060
Citazione:
M. Boyer et al., "Protein interactions in concentrated ribonuclease solutions", J CRYST GR, 196(2-4), 1999, pp. 185-192

Abstract

To investigate the protein interactions involved in the crystallization process of ribonuclease A, dynamic light scattering (DLS) and small angle X-ray scattering experiments (SAXS) were performed on concentrated solutions. Whereas the translational diffusion coefficient obtained from DLS is sensitive to thermodynamic and hydrodynamic interactions and permits to calculatean interaction parameter, the shape of the SAXS curves is related to the type of interaction (attractive or repulsive). We compared the effect of pH on protein interactions in the case of two types of crystallizing agents: amixture of salts (3 M sodium chloride plus 0.2 M ammonium sulfate) and an organic solvent (ethanol). The results show that in the presence of ethanol, as in low salt, protein interactions become more attractive as the pH increases from 4 to 8 and approaches the isoelectric point. In contrast, a reverse effect is observed in high salt conditions: the strength of attractiveinteractions decreases as the pH increases. The range of the pH effect canbe related to ionization of histidine residues, particularly those locatedin the active site of the protein. The present observations point out the important role played by localized charges in crystallization conditions, whatever the precipitating agent. (C) 1999 Elsevier Science B.V. All rights reserved.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 04/12/20 alle ore 20:09:12