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Crowding-Controlled Cluster Size in Concentrated Aqueous Protein Solutions : Structure, Self- and Collective Diffusion

Braun, Michal K. ; Grimaldo, Marco ; Roosen-Runge, Felix LU ; Hoffmann, Ingo ; Czakkel, Orsolya ; Sztucki, Michael ; Zhang, Fajun ; Schreiber, Frank and Seydel, Tilo (2017) In Journal of Physical Chemistry Letters 8(12). p.2590-2596
Abstract

We investigate the concentration-controlled formation of clusters in β-lactoglobulin (BLG) protein solutions combining structural and dynamical scattering techniques. The static structure factor from small-angle X-ray scattering as well as de-Gennes narrowing in the nanosecond diffusion function D(q) from neutron spin echo spectroscopy support a picture of cluster formation. Using neutron backscattering spectroscopy, a monotonous increase of the average hydrodynamic cluster radius is monitored over a broad protein concentration range, corresponding to oligomeric structures of BLG ranging from the native dimers up to roughly four dimers. The results suggest that BLG forms compact clusters that are static on the observation time scale of... (More)

We investigate the concentration-controlled formation of clusters in β-lactoglobulin (BLG) protein solutions combining structural and dynamical scattering techniques. The static structure factor from small-angle X-ray scattering as well as de-Gennes narrowing in the nanosecond diffusion function D(q) from neutron spin echo spectroscopy support a picture of cluster formation. Using neutron backscattering spectroscopy, a monotonous increase of the average hydrodynamic cluster radius is monitored over a broad protein concentration range, corresponding to oligomeric structures of BLG ranging from the native dimers up to roughly four dimers. The results suggest that BLG forms compact clusters that are static on the observation time scale of several nanoseconds. The presented analysis provides a general framework to access the structure and dynamics of macromolecular assemblies in solution.

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author
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organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Journal of Physical Chemistry Letters
volume
8
issue
12
pages
7 pages
publisher
The American Chemical Society (ACS)
external identifiers
  • wos:000403741800008
  • pmid:28525282
  • scopus:85020824333
ISSN
1948-7185
DOI
10.1021/acs.jpclett.7b00658
language
English
LU publication?
yes
id
512a062f-1629-4c15-83e1-b8e20a47587d
date added to LUP
2017-07-04 08:41:45
date last changed
2024-01-14 00:09:31
@article{512a062f-1629-4c15-83e1-b8e20a47587d,
  abstract     = {{<p>We investigate the concentration-controlled formation of clusters in β-lactoglobulin (BLG) protein solutions combining structural and dynamical scattering techniques. The static structure factor from small-angle X-ray scattering as well as de-Gennes narrowing in the nanosecond diffusion function D(q) from neutron spin echo spectroscopy support a picture of cluster formation. Using neutron backscattering spectroscopy, a monotonous increase of the average hydrodynamic cluster radius is monitored over a broad protein concentration range, corresponding to oligomeric structures of BLG ranging from the native dimers up to roughly four dimers. The results suggest that BLG forms compact clusters that are static on the observation time scale of several nanoseconds. The presented analysis provides a general framework to access the structure and dynamics of macromolecular assemblies in solution.</p>}},
  author       = {{Braun, Michal K. and Grimaldo, Marco and Roosen-Runge, Felix and Hoffmann, Ingo and Czakkel, Orsolya and Sztucki, Michael and Zhang, Fajun and Schreiber, Frank and Seydel, Tilo}},
  issn         = {{1948-7185}},
  language     = {{eng}},
  month        = {{06}},
  number       = {{12}},
  pages        = {{2590--2596}},
  publisher    = {{The American Chemical Society (ACS)}},
  series       = {{Journal of Physical Chemistry Letters}},
  title        = {{Crowding-Controlled Cluster Size in Concentrated Aqueous Protein Solutions : Structure, Self- and Collective Diffusion}},
  url          = {{http://dx.doi.org/10.1021/acs.jpclett.7b00658}},
  doi          = {{10.1021/acs.jpclett.7b00658}},
  volume       = {{8}},
  year         = {{2017}},
}