Nanosecond Tracer Diffusion as a Probe of the Solution Structure and Molecular Mobility of Protein Assemblies: The Case of Ovalbumin
(2018) In The Journal of Physical Chemistry Part 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)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/2efd2faa-d6d1-418b-8ba0-7beef93d82c1
- author
- Beck, Christian ; Grimaldo, Marco ; Roosen-Runge, Felix LU ; Braun, Michal K. ; Zhang, Fajun and Schreiber, Frank
- organization
- publishing date
- 2018
- type
- Contribution to journal
- publication status
- published
- subject
- in
- The Journal of Physical Chemistry Part B
- volume
- 122
- issue
- 35
- pages
- 8350 pages
- publisher
- The American Chemical Society (ACS)
- external identifiers
-
- pmid:30106587
- scopus:85052396644
- ISSN
- 1520-5207
- 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
- 2022-03-09 22:46:11
@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}},
issn = {{1520-5207}},
language = {{eng}},
number = {{35}},
pages = {{8343--8343}},
publisher = {{The American Chemical Society (ACS)}},
series = {{The Journal of Physical Chemistry Part 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}},
doi = {{10.1021/acs.jpcb.8b04349}},
volume = {{122}},
year = {{2018}},
}