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Structure of Escherichia coli dUTPase in Solution: A Small Angle Neutron Scattering Study

✍ Scribed by Beata G. Vertesse; Salvatore Magazù; Alfonso Mangione; Federica Migliardo; Astrid Brandt

Publisher
John Wiley and Sons
Year
2003
Tongue
English
Weight
243 KB
Volume
3
Category
Article
ISSN
1616-5187

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✦ Synopsis

Abstract

The present study investigates shape properties of the enzyme dUTPase from Escherichia coli in the solution phase. In this work small angle neutron scattering (SANS) findings on dUTPase/D~2~O solutions for temperature values of T = 8 °C and T = 37 °C are presented. The analysis of SANS data, carried out by using a prolate ellipsoid core/shell model fitting and the well‐known Guinier and Zimm analysis procedures allows the characterization of the shape of the protein in solution. By means of the comparison with experimental and theoretical data existing in literature on dUTPase in the crystalline state, we find that the protein in solution maintains its dimensions before the denaturation process. Furthermore, by analyzing the SANS spectra of dUTPase/D~2~O/trehalose solutions, we emphasize the bioprotective effects of trehalose on the protein.

Structure of dUTPase.

magnified imageStructure of dUTPase.

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