Structure of Escherichia coli dUTPase in solution: A small angle neutron scattering study

Beata G. Vertesse, Salvatore Magazù, Alfonso Mangione, Federica Migliardo, Astrid Brandt

Research output: Contribution to journalArticle

6 Citations (Scopus)


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/D2O 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/D2O/trehalose solutions, we emphasize the bioprotective effects of trehalose on the protein.

Original languageEnglish
Pages (from-to)477-481
Number of pages5
JournalMacromolecular Bioscience
Issue number9
Publication statusPublished - Sep 10 2003


  • Conformational analysis
  • Neutron scattering
  • Proteins
  • Stabilization

ASJC Scopus subject areas

  • Biotechnology
  • Bioengineering
  • Biomaterials
  • Polymers and Plastics
  • Materials Chemistry

Fingerprint Dive into the research topics of 'Structure of Escherichia coli dUTPase in solution: A small angle neutron scattering study'. Together they form a unique fingerprint.

  • Cite this