Journal
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Volume 108, Issue 29, Pages 11815-11820Publisher
NATL ACAD SCIENCES
DOI: 10.1073/pnas.1107287108
Keywords
macromolecular crowding; quasi-elastic neutron scattering; globular proteins
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- ILL
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Macromolecular crowding in biological media is an essential factor for cellular function. The interplay of intermolecular interactions at multiple time and length scales governs a fine-tuned system of reaction and transport processes, including particularly protein diffusion as a limiting or driving factor. Using quasielastic neutron backscattering, we probe the protein self-diffusion in crowded aqueous solutions of bovine serum albumin on nanosecond time and nanometer length scales employing the same protein as crowding agent. The measured diffusion coefficient D(phi) strongly decreases with increasing protein volume fraction phi explored within 7% <= phi <= 30%. With an ellipsoidal protein model and an analytical framework involving colloid diffusion theory, we separate the rotational D-r(phi) and translational D-t(phi) contributions to D(phi). The resulting D-t(phi) is described by short-time self-diffusion of effective spheres. Protein self-diffusion at biological volume fractions is found to be slowed down to 20% of the dilute limit solely due to hydrodynamic interactions.
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