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Titolo:
EVIDENCE FOR A DIMERIC INTERMEDIATE ON THE CRYSTALLIZATION PATHWAY OFRIBONUCLEASE-A
Autore:
JULLIEN M; CROSIO MP; BAUDETNESSLER S; MEROLA F; BROCHON JC;
Indirizzi:
UNIV MONTPELLIER 1,FAC PHARM,CTR BIOCHIM STRUCT,UNITE MIXTE RECH C9955,CNRS F-34060 MONTPELLIER 1 FRANCE LAB BIOL STRUCT F-91405 ORSAY FRANCE LAB UTILISAT RAYONNEMENT SYNCHROTRON F-91405 ORSAY FRANCE
Titolo Testata:
Acta crystallographica. Section D, Biological crystallography
, volume: 50, anno: 1994,
parte:, 4
pagine: 398 - 403
SICI:
0907-4449(1994)50:<398:EFADIO>2.0.ZU;2-E
Fonte:
ISI
Lingua:
ENG
Soggetto:
CRYSTAL-STRUCTURE; SEMISYNTHETIC RIBONUCLEASE; FLUORESCENT-PROBE; PRECRYSTALLIZATION; NUCLEATION; GROWTH;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
20
Recensione:
Indirizzi per estratti:
Citazione:
M. Jullien et al., "EVIDENCE FOR A DIMERIC INTERMEDIATE ON THE CRYSTALLIZATION PATHWAY OFRIBONUCLEASE-A", Acta crystallographica. Section D, Biological crystallography, 50, 1994, pp. 398-403

Abstract

Early steps in the crystallization process of pancreatic ribonucleasehave been investigated by time-dependent fluorescence anisotropy, using a labeled protein as a fluorescent probe. Previous experiments haveshown that steady-state fluorescence anisotropy is sensitive to protein-protein interactions and can be used to find new crystallization conditions. The present work describes an attempt, by means of time-resolved experiments, to detect and characterize species appearing in the early stages of the crystallization pathway. Fluorescence anisotropy decay was measured with synchrotron radiation as a light source under avariety of conditions where it is known that the solutions tend towards crystallization; the decay was analyzed by a maximum-entropy methodthat calculates a rotational correlation-time distribution. Fluorescence anisotropy originates in the Brownian rotatory motion of macromolecules and the values of the correlation times are related to the size and shape of different species present in the solution. In the presence of high salt concentrations, a bimodal distribution is always observed. Whereas a peak of protein monomer is still present, a second peak appears as a stable intermediate in the crystallization pathway. The correlation time of this new species varies between two and three timesthe correlation time of the monomer. The second peak is possibly the symmetrical dimer of the ribonuclease molecules commonly observed in all the high-salt crystal forms.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 01/12/20 alle ore 16:33:42