<i>In Vivo</i> Protein Dynamics on the Nanometer Length Scale and Nanosecond Time Scale [electronic resource].
- Washington, D.C. : United States. Dept. of Energy. Office of Science, 2017. and Oak Ridge, Tenn. : Distributed by the Office of Scientific and Technical Information, U.S. Dept. of Energy
- Physical Description:
- pages 1,899-1,904 : digital, PDF file
- Additional Creators:
- Oak Ridge National Laboratory, United States. Department of Energy. Office of Science, and United States. Department of Energy. Office of Scientific and Technical Information
- Restrictions on Access:
- Free-to-read Unrestricted online access
- Selectively labeled GroEL protein was produced in living deuterated bacterial cells to enhance its neutron scattering signal above that of the intracellular milieu. Quasi-elastic neutron scattering shows that the in-cell diffusion coefficient of GroEL was (4.7 ± 0.3) × 10<sup>–12</sup> m<sup>2</sup>/s, a factor of 4 slower than its diffusion coefficient in buffer solution. Furthermore, for internal protein dynamics we see a relaxation time of (65 ± 6) ps, a factor of 2 slower compared to the protein in solution. Comparison to the literature suggests that the effective diffusivity of proteins depends on the length and time scale being probed. Retardation of in-cell diffusion compared to the buffer becomes more significant with the increasing probe length scale, suggesting that intracellular diffusion of biomolecules is nonuniform over the cellular volume. This approach outlined here enables investigation of protein dynamics within living cells to open up new lines of research using “in-cell neutron scattering” to study the dynamics of complex biomolecular systems.
- Published through SciTech Connect., 04/07/2017., "73038", Journal of Physical Chemistry Letters 8 8 ISSN 1948-7185 AM, and Divina B. Anunciado; Vyncent P. Nyugen; Gregory B. Hurst; Mitchel J. Doktycz; Volker Urban; Paul Langan; Eugene Mamontov; Hugh O’Neill.
- Funding Information:
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