Research ArticleBIOPHYSICS

Determination of functional collective motions in a protein at atomic resolution using coherent neutron scattering

Science Advances  14 Oct 2016:
Vol. 2, no. 10, e1600886
DOI: 10.1126/sciadv.1600886

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Protein function often depends on global, collective internal motions. However, the simultaneous quantitative experimental determination of the forms, amplitudes, and time scales of these motions has remained elusive. We demonstrate that a complete description of these large-scale dynamic modes can be obtained using coherent neutron-scattering experiments on perdeuterated samples. With this approach, a microscopic relationship between the structure, dynamics, and function in a protein, cytochrome P450cam, is established. The approach developed here should be of general applicability to protein systems.

  • Protein dynamics
  • coherent neutron scattering
  • molecular dynamics simulation
  • normal mode analysis
  • collective motion

This is an open-access article distributed under the terms of the Creative Commons Attribution-NonCommercial license, which permits use, distribution, and reproduction in any medium, so long as the resultant use is not for commercial advantage and provided the original work is properly cited.

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