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 journalArticlepeer-review

19 Scopus citations

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 languageEnglish
Pages (from-to)243-256
Number of pages14
JournalJournal of Molecular Structure
Volume519
Issue number1-3
DOIs
StatePublished - 29 Feb 2000
Externally publishedYes

Keywords

  • Dynamic light scattering
  • Geometrical factor
  • Human apolipoproteins
  • Protein crystallization
  • Turbidity

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