Turbidity as a useful optical parameter to predict protein crystallization by dynamic light scattering

A. Moreno, J. Mas-Oliva, M. Soriano-García, C. Oliver Salvador, V. Martín Bolaños-García

Research output: Contribution to journalArticleResearchpeer-review

17 Citations (Scopus)

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 (τ) under different environmental conditions, is a useful approach in order to elucidate if protein aggregation is carried 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 r are taken into account. (C) 2000 Elsevier Science B.V.
Original languageAmerican English
Pages (from-to)243-256
Number of pages217
JournalJournal of Molecular Structure
DOIs
StatePublished - 29 Feb 2000
Externally publishedYes

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turbidity
Dynamic light scattering
Turbidity
Crystallization
light scattering
crystallization
proteins
Agglomeration
Complement Factor H
Proteins
lysozyme
Muramidase
Concanavalin A
Nucleation
nucleation

Cite this

Moreno, A. ; Mas-Oliva, J. ; Soriano-García, M. ; Oliver Salvador, C. ; Martín Bolaños-García, V. / Turbidity as a useful optical parameter to predict protein crystallization by dynamic light scattering. In: Journal of Molecular Structure. 2000 ; pp. 243-256.
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Turbidity as a useful optical parameter to predict protein crystallization by dynamic light scattering. / Moreno, A.; Mas-Oliva, J.; Soriano-García, M.; Oliver Salvador, C.; Martín Bolaños-García, V.

In: Journal of Molecular Structure, 29.02.2000, p. 243-256.

Research output: Contribution to journalArticleResearchpeer-review

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