Published October 12, 2005 | Version v1
Journal article

Pressure dependence of protein dynamics investigated using elastic and quasielastic neutron scattering

  • 1. Dipartimento di Fisica and Istituto Nazionale per la Fisica della Materia, Universita di Roma 'Tor Vergata', Via della Ricerca Scientifica 1, I-00133 Rome (Italy)
  • 2. Dipartimento di Fisica and Istituto Nazionale per la Fisica della Materia, Universita di Parma, Parco Area delle Scienze 7/A, I-43100 Parma (Italy)
  • 3. Dipartimento di Medicina Sperimentale e Scienze Biochimiche and Istituto Nazionale per la Fisica della Materia, Universita di Roma 'Tor Vergata', Via Montpellier 1, I-00133 Rome (Italy)

Description

We present here a study of the dynamics of two monomeric proteins, trypsin and lysozyme, by means of elastic and quasielastic neutron scattering under medium-to-high pressure conditions (1-1200 bar). The internal motions as probed from the average proton dynamics in the 100 ps timescale have a confined diffusive nature. On increasing the pressure up to 1200 bar the confinement volume is almost unaffected, while the fraction of protons involved is slightly decreased

Availability note (English)

Available online at http://stacks.iop.org/0953-8984/17/S3101/cm5_40_013.pdf or at the Web site for the Journal of Physics. Condensed Matter (ISSN 1361-648X) http://www.iop.org/

Additional details

Publishing Information

Journal Title
Journal of Physics. Condensed Matter
Journal Volume
17
Journal Issue
40
Journal Page Range
p. S3101-S3109
ISSN
0953-8984
CODEN
JCOMEL