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

ABSTRACT: 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.

SUBMITTER: Hong L

PROVIDER: S-EPMC5065251 | biostudies-literature | 2016 Oct

REPOSITORIES: biostudies-literature

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

Hong Liang L Jain Nitin N Cheng Xiaolin X Bernal Ana A Tyagi Madhusudan M Smith Jeremy C JC

Science advances 20161014 10

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, cytochrom ...[more]

PMID: 27757419

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