Effects of Protein Purity and Precipitant Stereochemistry on the Crystallization of Thaumatin

Autor:	Arieh Greenbaum, Sarah Knafo, Samuel Blass, Neer Asherie, Charles Ginsberg
Rok vydání:	2008
Předmět:	Stereochemistry food and beverages Model protein General Chemistry Tartrate Condensed Matter Physics law.invention chemistry.chemical_compound Crystallography chemistry Thaumatin Homogeneous law General Materials Science Solubility Crystallization Enantiomer Protein solubility
Zdroj:	Crystal Growth & Design. 8:4200-4207
ISSN:	1528-7505 1528-7483
DOI:	10.1021/cg800616q
Popis:	Thaumatin is frequently used as a model protein in crystallization studies because it rapidly forms crystals in the presence of tartrate ions. The thermodynamic and kinetic properties of thaumatin crystals have been studied for almost 10 years, and the results are contradictory. Here we show that by using a homogeneous preparation of thaumatin and controlling the stereochemistry of the tartrate precipitant, it is possible to achieve consistent results for the protein solubility. To understand the role of protein impurities in the crystallization of thaumatin, we examined two commercial sources of the protein and characterized the heterogeneities therein. To examine the effect of precipitant stereochemistry, we crystallized thaumatin with l, d, and dl (racemic) tartrate ions. We suggest that the inconsistencies among previous results stem in part from the different behavior of thaumatin with the l and d enantiomers: the solubility of thaumatin crystals increases with temperature in l-tartrate, whereas it d...
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_________::657067a1937c8cfe787ce4b3c7fcec94 https://doi.org/10.1021/cg800616q Zobrazit plný text záznamu