Protein dynamics by neutron scattering: The protein dynamical transition and the fragile-to-strong dynamical crossover in hydrated lysozyme

Salvatore Magazù, Federica Migliardo, Antonio Benedetto, B. Vértessy

Research output: Contribution to journalArticle

6 Citations (Scopus)

Abstract

In this work Elastic Incoherent Neutron Scattering (EINS) results on lysozyme water mixtures in absence and in presence of bioprotectant systems are presented. The EINS data have been collected by using the IN13 and the IN10 spectrometers at the Institut Laue-Langevin (ILL, Grenoble, France) allowing to evaluate the temperature behaviour of the mean square displacement and of the relaxation time for the investigated systems. The obtained experimental findings together with theoretical calculations allow to put into evidence the role played by the spectrometer resolution and to clarify the connexion between the registered protein dynamical transition, the system relaxation time, and the instrumental energy resolution.

Original languageEnglish
Pages (from-to)26-31
Number of pages6
JournalChemical Physics
Volume424
DOIs
Publication statusPublished - 2013

Fingerprint

Incoherent scattering
incoherent scattering
lysozyme
Muramidase
Neutron scattering
Relaxation time
Spectrometers
crossovers
neutron scattering
relaxation time
spectrometers
proteins
France
Proteins
Water
water
Temperature
temperature
energy

Keywords

  • Bioprotectant
  • Dynamical transition
  • Elastic neutron scattering
  • Lysozyme
  • Mean square displacement
  • Resolution effects
  • Vibrational motion amplitude

ASJC Scopus subject areas

  • Physical and Theoretical Chemistry
  • Physics and Astronomy(all)

Cite this

Protein dynamics by neutron scattering : The protein dynamical transition and the fragile-to-strong dynamical crossover in hydrated lysozyme. / Magazù, Salvatore; Migliardo, Federica; Benedetto, Antonio; Vértessy, B.

In: Chemical Physics, Vol. 424, 2013, p. 26-31.

Research output: Contribution to journalArticle

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