de Gennes narrowing describes the relative motion of protein domains

Hong, Liang; Smolin, Nikolai; Smith, Jeremy C.

doi:10.1103/PhysRevLett.112.158102

Title: de Gennes narrowing describes the relative motion of protein domains

Journal Article · Fri Apr 18 00:00:00 EDT 2014 · Physical Review Letters

DOI:https://doi.org/10.1103/PhysRevLett.112.158102· OSTI ID:1265924

Hong, Liang ^[1]; Smolin, Nikolai ^[2]; Smith, Jeremy C. ^[1]

Oak Ridge National Lab. (ORNL), Oak Ridge, TN (United States); Univ. of Tennessee, Knoxville, TN (United States)
Oak Ridge National Lab. (ORNL), Oak Ridge, TN (United States); Loyola Univ. Chicago, Maywood, IL (United States)

The relative motion of structural domains is essential for the biological function of many proteins. Here, by analyzing neutron scattering data and performing molecular dynamics simulations, we find that interdomain motion in several proteins obeys the principle of de Gennes narrowing, in which the wave vector dependence of the interdomain diffusion coefficient is inversely proportional to the interdomain structure factor. Furthermore, the rate of interdomain motion is inversely proportional to the probability distribution of the spatial configurations of domains.

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Research Organization:: Oak Ridge National Lab. (ORNL), Oak Ridge, TN (United States). Oak Ridge Leadership Computing Facility (OLCF)

Sponsoring Organization:: USDOE Office of Science (SC); USDOE Laboratory Directed Research and Development (LDRD) Program

DOE Contract Number:: AC05-00OR22725

OSTI ID:: 1265924

Journal Information:: Physical Review Letters, Vol. 112, Issue 15; ISSN 0031-9007

Publisher:: American Physical Society (APS)

Country of Publication:: United States

Language:: English

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