Journal of Biological Physics

, Volume 36, Issue 2, pp 207–220

Study of solvent–protein coupling effects by neutron scattering

  • B. Varga
  • F. Migliardo
  • E. Takacs
  • B. Vertessy
  • Salvatore Magazù
  • M. T. F. Telling
Original Paper

DOI: 10.1007/s10867-009-9177-5

Cite this article as:
Varga, B., Migliardo, F., Takacs, E. et al. J Biol Phys (2010) 36: 207. doi:10.1007/s10867-009-9177-5

Abstract

The present work aims to characterize the dynamical behavior of proteins immersed in bio-preserving liquids and glasses. For this purpose, the protein dUTPase was chosen, while the selected solvents were glycerol, a triol, and some homologous disaccharides, i.e., trehalose, maltose, and sucrose, which are known to be very effective bio-preserving agents. The results highlight that the disaccharides show a slowing down effect on the water dynamics, which is stronger for trehalose than in the case of the other disaccharides. Furthermore, a characterization of the medium which hosts the protein is performed by using an operative definition of fragility based on the mean square displacement extracted by elastic incoherent neutron scattering, which is directly connected to Angell’s kinetic fragility based on the viscosity. Finally, a study of the dynamics of the protein sequestered within the solvents is performed. The result shows that the protein dynamics is coupled with that of the surrounding matrix.

Keywords

Quasi-elastic neutron scattering Elastic neutron scattering Protein Bioprotection 

Copyright information

© Springer Science+Business Media B.V. 2009

Authors and Affiliations

  • B. Varga
    • 1
  • F. Migliardo
    • 2
    • 3
  • E. Takacs
    • 1
  • B. Vertessy
    • 1
  • Salvatore Magazù
    • 2
  • M. T. F. Telling
    • 4
  1. 1.Institute of EnzymologyHungarian Academy of SciencesBudapestHungary
  2. 2.Dipartimento di FisicaUniversità di MessinaMessinaItaly
  3. 3.Laboratoire de Dynamique et Structure des Matériaux MoléculairesUniversity of Lille 1Villeneuve d’Ascq CEDEXFrance
  4. 4.ISIS FacilityRutherford Appleton LaboratoryOxonUK

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