Diffusion and dynamics of γ-globulin in crowded aqueous solutions
(2014) In Journal of Physical Chemistry B 118(25). p.7203-7209- Abstract
Dynamics in protein solutions is essential for both protein function and cellular processes. The hierarchical complexity of global protein diffusion, side-chain diffusion, and microscopic motions of chemical groups renders a complete understanding challenging. We present results from quasi-elastic neutron scattering on protein solutions of γ-globulin over a wide range of volume fractions. Translational and rotational diffusion can be self-consistently separated from internal motions. The global diffusion is consistent with predictions for effective spheres even though the branched molecular shape differs considerably from a colloidal sphere. The internal motions are characterized both geometrically and dynamically, suggesting a picture... (More)
Dynamics in protein solutions is essential for both protein function and cellular processes. The hierarchical complexity of global protein diffusion, side-chain diffusion, and microscopic motions of chemical groups renders a complete understanding challenging. We present results from quasi-elastic neutron scattering on protein solutions of γ-globulin over a wide range of volume fractions. Translational and rotational diffusion can be self-consistently separated from internal motions. The global diffusion is consistent with predictions for effective spheres even though the branched molecular shape differs considerably from a colloidal sphere. The internal motions are characterized both geometrically and dynamically, suggesting a picture of methyl rotations and restricted diffusion of side chains. We show that the advent of new neutron spectrometers allows the study of current questions including the coupling of intracellular dynamics and protein function.
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- author
- Grimaldo, Marco ; Roosen-Runge, Felix LU ; Zhang, Fajun ; Seydel, Tilo and Schreiber, Frank
- publishing date
- 2014-06-26
- type
- Contribution to journal
- publication status
- published
- in
- Journal of Physical Chemistry B
- volume
- 118
- issue
- 25
- pages
- 7 pages
- publisher
- The American Chemical Society (ACS)
- external identifiers
-
- scopus:84903467284
- pmid:24871685
- ISSN
- 1520-6106
- DOI
- 10.1021/jp504135z
- language
- English
- LU publication?
- no
- id
- a90083a5-e73a-4aab-9d7e-dd2e329211b3
- date added to LUP
- 2018-12-17 09:48:14
- date last changed
- 2025-06-27 00:37:13
@article{a90083a5-e73a-4aab-9d7e-dd2e329211b3,
abstract = {{<p>Dynamics in protein solutions is essential for both protein function and cellular processes. The hierarchical complexity of global protein diffusion, side-chain diffusion, and microscopic motions of chemical groups renders a complete understanding challenging. We present results from quasi-elastic neutron scattering on protein solutions of γ-globulin over a wide range of volume fractions. Translational and rotational diffusion can be self-consistently separated from internal motions. The global diffusion is consistent with predictions for effective spheres even though the branched molecular shape differs considerably from a colloidal sphere. The internal motions are characterized both geometrically and dynamically, suggesting a picture of methyl rotations and restricted diffusion of side chains. We show that the advent of new neutron spectrometers allows the study of current questions including the coupling of intracellular dynamics and protein function.</p>}},
author = {{Grimaldo, Marco and Roosen-Runge, Felix and Zhang, Fajun and Seydel, Tilo and Schreiber, Frank}},
issn = {{1520-6106}},
language = {{eng}},
month = {{06}},
number = {{25}},
pages = {{7203--7209}},
publisher = {{The American Chemical Society (ACS)}},
series = {{Journal of Physical Chemistry B}},
title = {{Diffusion and dynamics of γ-globulin in crowded aqueous solutions}},
url = {{http://dx.doi.org/10.1021/jp504135z}},
doi = {{10.1021/jp504135z}},
volume = {{118}},
year = {{2014}},
}