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Protein dynamics studied by neutron scattering

Journal Article


Abstract


  • This review of protein dynamics studied by neutron scattering focuses on data collected in the last 10 years. After an introduction to thermal neutron scattering and instrumental aspects, theoretical models that have been used to interpret the data are presented and discussed. Experiments are described according to sample type, protein powders, solutions and membranes. Neutron-scattering results are compared to those obtained from other techniques. The biological relevance of the experimental results is discussed. The major conclusion of the last decade concerns the strong dependence of internal dynamics on the macromolecular environment.

Publication Date


  • 2002

Citation


  • Gabel, F., Bicout, D., Lehnert, U., Tehei, M., Weik, M., & Zaccai, G. (2002). Protein dynamics studied by neutron scattering. Quarterly Reviews of Biophysics, 35(4), 327-367. doi:10.1017/S0033583502003840

Scopus Eid


  • 2-s2.0-0036880187

Start Page


  • 327

End Page


  • 367

Volume


  • 35

Issue


  • 4

Place Of Publication


Abstract


  • This review of protein dynamics studied by neutron scattering focuses on data collected in the last 10 years. After an introduction to thermal neutron scattering and instrumental aspects, theoretical models that have been used to interpret the data are presented and discussed. Experiments are described according to sample type, protein powders, solutions and membranes. Neutron-scattering results are compared to those obtained from other techniques. The biological relevance of the experimental results is discussed. The major conclusion of the last decade concerns the strong dependence of internal dynamics on the macromolecular environment.

Publication Date


  • 2002

Citation


  • Gabel, F., Bicout, D., Lehnert, U., Tehei, M., Weik, M., & Zaccai, G. (2002). Protein dynamics studied by neutron scattering. Quarterly Reviews of Biophysics, 35(4), 327-367. doi:10.1017/S0033583502003840

Scopus Eid


  • 2-s2.0-0036880187

Start Page


  • 327

End Page


  • 367

Volume


  • 35

Issue


  • 4

Place Of Publication