Protein self-diffusion in crowded solutions
(2011) In Proceedings of the National Academy of Sciences of the United States of America 108(29). p.11815-11820- Abstract
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(φ) strongly decreases with increasing protein volume fraction χ explored within 7% ≤ φ ≤ 30%. With an ellipsoidal protein model and an analytical framework involving colloid... (More)
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(φ) strongly decreases with increasing protein volume fraction χ explored within 7% ≤ φ ≤ 30%. With an ellipsoidal protein model and an analytical framework involving colloid diffusion theory, we separate the rotational D r (φ) and translational D t(φ) contributions to D(φ). The resulting D t(φ) 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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- author
- Roosen-Runge, Felix LU ; Hennig, Marcus ; Zhang, Fajun ; Jacobs, Robert M J ; Sztucki, Michael ; Schober, Helmut ; Seydel, Tilo and Schreiber, Frank
- publishing date
- 2011-07-19
- type
- Contribution to journal
- publication status
- published
- keywords
- Globular proteins, Macromolecular crowding, Quasi-elastic neutron scattering
- in
- Proceedings of the National Academy of Sciences of the United States of America
- volume
- 108
- issue
- 29
- pages
- 6 pages
- publisher
- National Academy of Sciences
- external identifiers
-
- pmid:21730176
- scopus:79961065566
- ISSN
- 0027-8424
- DOI
- 10.1073/pnas.1107287108
- language
- English
- LU publication?
- no
- id
- 80e784b3-822a-42ef-978d-6d961b1e4aeb
- date added to LUP
- 2018-12-17 09:50:11
- date last changed
- 2024-09-18 09:24:55
@article{80e784b3-822a-42ef-978d-6d961b1e4aeb,
abstract = {{<p>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(φ) strongly decreases with increasing protein volume fraction χ explored within 7% ≤ φ ≤ 30%. With an ellipsoidal protein model and an analytical framework involving colloid diffusion theory, we separate the rotational D <sub>r</sub> (φ) and translational D <sub>t</sub>(φ) contributions to D(φ). The resulting D <sub>t</sub>(φ) 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.</p>}},
author = {{Roosen-Runge, Felix and Hennig, Marcus and Zhang, Fajun and Jacobs, Robert M J and Sztucki, Michael and Schober, Helmut and Seydel, Tilo and Schreiber, Frank}},
issn = {{0027-8424}},
keywords = {{Globular proteins; Macromolecular crowding; Quasi-elastic neutron scattering}},
language = {{eng}},
month = {{07}},
number = {{29}},
pages = {{11815--11820}},
publisher = {{National Academy of Sciences}},
series = {{Proceedings of the National Academy of Sciences of the United States of America}},
title = {{Protein self-diffusion in crowded solutions}},
url = {{http://dx.doi.org/10.1073/pnas.1107287108}},
doi = {{10.1073/pnas.1107287108}},
volume = {{108}},
year = {{2011}},
}