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Nanosecond Tracer Diffusion as a Probe of the Solution Structure and Molecular Mobility of Protein Assemblies: The Case of Ovalbumin

Beck, Christian; Grimaldo, Marco; Roosen-Runge, Felix LU ; Braun, Michal K.; Zhang, Fajun and Schreiber, Frank (2018) In The Journal of Physical Chemistry B 122(35). p.8343-8343
Abstract
Protein diffusion is not only an important process ensuring biological function but can also be used as a probe to obtain information on structural properties of protein assemblies in liquid solutions. Here, we explore the oligomerization state of ovalbumin at high protein concentrations by means of its short-time self-diffusion. We employ high-resolution incoherent quasielastic neutron scattering to access the self-diffusion on nanosecond timescales, on which interparticle contacts are not altered. Our results indicate that ovalbumin in aqueous (D2O) solutions occurs in increasingly large assemblies of its monomeric subunits with rising protein concentration. It changes from nearly monomeric toward dimeric and ultimately larger than... (More)
Protein diffusion is not only an important process ensuring biological function but can also be used as a probe to obtain information on structural properties of protein assemblies in liquid solutions. Here, we explore the oligomerization state of ovalbumin at high protein concentrations by means of its short-time self-diffusion. We employ high-resolution incoherent quasielastic neutron scattering to access the self-diffusion on nanosecond timescales, on which interparticle contacts are not altered. Our results indicate that ovalbumin in aqueous (D2O) solutions occurs in increasingly large assemblies of its monomeric subunits with rising protein concentration. It changes from nearly monomeric toward dimeric and ultimately larger than tetrameric complexes. Simultaneously, we access information on the internal molecular mobility of ovalbumin on the nanometer length scale and compare it with results obtained for bovine serum albumin, immunoglobulin, and β-lactoglobulin. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
The Journal of Physical Chemistry B
volume
122
issue
35
pages
8350 pages
publisher
The American Chemical Society
external identifiers
  • scopus:85052396644
DOI
10.1021/acs.jpcb.8b04349
language
English
LU publication?
yes
id
2efd2faa-d6d1-418b-8ba0-7beef93d82c1
date added to LUP
2018-11-28 16:08:22
date last changed
2019-08-14 04:28:31
@article{2efd2faa-d6d1-418b-8ba0-7beef93d82c1,
  abstract     = {Protein diffusion is not only an important process ensuring biological function but can also be used as a probe to obtain information on structural properties of protein assemblies in liquid solutions. Here, we explore the oligomerization state of ovalbumin at high protein concentrations by means of its short-time self-diffusion. We employ high-resolution incoherent quasielastic neutron scattering to access the self-diffusion on nanosecond timescales, on which interparticle contacts are not altered. Our results indicate that ovalbumin in aqueous (D2O) solutions occurs in increasingly large assemblies of its monomeric subunits with rising protein concentration. It changes from nearly monomeric toward dimeric and ultimately larger than tetrameric complexes. Simultaneously, we access information on the internal molecular mobility of ovalbumin on the nanometer length scale and compare it with results obtained for bovine serum albumin, immunoglobulin, and β-lactoglobulin.},
  author       = {Beck, Christian and Grimaldo, Marco and Roosen-Runge, Felix and Braun, Michal K. and Zhang, Fajun and Schreiber, Frank},
  language     = {eng},
  number       = {35},
  pages        = {8343--8343},
  publisher    = {The American Chemical Society},
  series       = {The Journal of Physical Chemistry B},
  title        = {Nanosecond Tracer Diffusion as a Probe of the Solution Structure and Molecular Mobility of Protein Assemblies: The Case of Ovalbumin},
  url          = {http://dx.doi.org/10.1021/acs.jpcb.8b04349},
  volume       = {122},
  year         = {2018},
}