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Titolo:
Turbidity as a useful optical parameter to predict protein crystallizationby dynamic light scattering
Autore:
Moreno, A; Mas-Oliva, J; Soriano-Garcia, M; Salvador, CO; Bolanos-Garcia, VM;
Indirizzi:
Univ Nacl Autonoma Mexico, Inst Quim, Dept Bioquim, Mexico City 04510, DF,Mexico Univ Nacl Autonoma Mexico Mexico City DF Mexico 04510 ty 04510, DF,Mexico Univ Nacl Autonoma Mexico, Inst Fisiol Celular, Dept Bioquim, Mexico City 04510, DF, Mexico Univ Nacl Autonoma Mexico Mexico City DF Mexico 04510 y 04510, DF, Mexico Univ Profes Interdisciplinaria Biotecnol, IPN, Mexico City, DF, Mexico Univ Profes Interdisciplinaria Biotecnol Mexico City DF Mexico F, Mexico
Titolo Testata:
JOURNAL OF MOLECULAR STRUCTURE
, volume: 519, anno: 2000,
pagine: 243 - 256
SICI:
0022-2860(20000229)519:<243:TAAUOP>2.0.ZU;2-1
Fonte:
ISI
Lingua:
ENG
Soggetto:
SUPERSATURATED LYSOZYME SOLUTIONS; GEL ACUPUNCTURE METHOD; 3-DIMENSIONAL STRUCTURE; VAPOR-DIFFUSION; CRYSTAL-GROWTH; PRECRYSTALLIZATION; MICROBATCH; MACROMOLECULES; BINDING; RATES;
Keywords:
dynamic light scattering; protein crystallization; turbidity; geometrical factor; human apolipoproteins;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Physical, Chemical & Earth Sciences
Citazioni:
38
Recensione:
Indirizzi per estratti:
Indirizzo: Bolanos-Garcia, VM Univ Cambridge, Dept Biochem, 80 Tennis Court Rd, Cambridge CB2 1GA, England Univ Cambridge 80 Tennis Court Rd Cambridge England CB2 1GA
Citazione:
A. Moreno et al., "Turbidity as a useful optical parameter to predict protein crystallizationby dynamic light scattering", J MOL STRUC, 519, 2000, pp. 243-256

Abstract

The aggregation behavior of several proteins in solution including the human apolipoproteins A-II and C-III, as well as concanavalin A, thaumatin, lysozyme and mexicain, is discussed based on dynamic light scattering techniques. According to our results, the estimation of parameters such as the geometrical factor (H) and turbidity (tau) under different environmental conditions, is a useful approach in order to elucidate if protein aggregation iscarried out by either nucleation or random mechanisms. We conclude that dynamic light scattering, an accurate and non-destructive technique, can be used to determine either protein precrystallization parameters or crystallization conditions when both H and tau are taken into account. (C) 2000 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 26/09/20 alle ore 02:04:38