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Titolo:
DYNAMIC LIGHT-SCATTERING STUDY OF PRECRYSTALLIZING RIBONUCLEASE SOLUTIONS
Autore:
BOYER M; ROY MO; JULLIEN M;
Indirizzi:
UNIV MONTPELLIER 1,FAC PHARM,CTR BIOCHIM STRUCT,CNRS,UMR C9955,INSERMU414 F-34060 MONTPELLIER FRANCE UNIV MONTPELLIER 1,FAC PHARM,CTR BIOCHIM STRUCT,CNRS,UMR C9955,INSERMU414 F-34060 MONTPELLIER FRANCE
Titolo Testata:
Journal of crystal growth
fascicolo: 1-2, volume: 167, anno: 1996,
pagine: 212 - 220
SICI:
0022-0248(1996)167:1-2<212:DLSOPR>2.0.ZU;2-Z
Fonte:
ISI
Lingua:
ENG
Soggetto:
PROTEIN CRYSTALLIZATION; CORRELATION SPECTROSCOPY; LYSOZYME SOLUTIONS; SOLUBILITY; MOLECULES; DIFFUSION; PARTICLES;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
33
Recensione:
Indirizzi per estratti:
Citazione:
M. Boyer et al., "DYNAMIC LIGHT-SCATTERING STUDY OF PRECRYSTALLIZING RIBONUCLEASE SOLUTIONS", Journal of crystal growth, 167(1-2), 1996, pp. 212-220

Abstract

The translational diffusion coefficient of bovine pancreatic ribonuclease A, a globular protein, has been measured by dynamic light scattering under various conditions related to the crystallization process. In all cases, a monomodal light scattering autocorrelation function wasobserved. The diffusion coefficient exhibited a linear dependence on protein concentration and an interaction parameter could be calculated. Attractive interactions were found to increase with salt concentration and to decrease with pH in the presence of salts. Finally, optimal crystallization conditions correspond to moderate attractive interactions.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 22/10/20 alle ore 09:20:37