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MOESM1 of Tension wood structure and morphology conducive for better enzymatic digestion
Additional file 1. Additional table and figures
<i>In Vivo</i> Protein Dynamics on the Nanometer Length Scale and Nanosecond Time Scale
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. Internal protein
dynamics showed 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. The 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