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Crowding-Controlled...
Crowding-Controlled Cluster Size in Concentrated Aqueous Protein Solutions : Structure, Self- and Collective Diffusion
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- Braun, Michal K. (författare)
- University of Tübingen
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- Grimaldo, Marco (författare)
- University of Tübingen,Institut Laue Langevin
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- Roosen-Runge, Felix (författare)
- Lund University,Lunds universitet,Fysikalisk kemi,Enheten för fysikalisk och teoretisk kemi,Kemiska institutionen,Institutioner vid LTH,Lunds Tekniska Högskola,Physical Chemistry,Physical and theoretical chemistry,Department of Chemistry,Departments at LTH,Faculty of Engineering, LTH,Institut Laue Langevin
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- Hoffmann, Ingo (författare)
- Institut Laue Langevin
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- Czakkel, Orsolya (författare)
- Institut Laue Langevin
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- Sztucki, Michael (författare)
- European Synchrotron Radiation Facility
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- Zhang, Fajun (författare)
- University of Tübingen
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- Schreiber, Frank (författare)
- University of Tübingen
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- Seydel, Tilo (författare)
- Institut Laue Langevin
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(creator_code:org_t)
- 2017-05-30
- 2017
- Engelska 7 s.
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Ingår i: Journal of Physical Chemistry Letters. - : American Chemical Society (ACS). - 1948-7185. ; 8:12, s. 2590-2596
- Relaterad länk:
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http://dx.doi.org/10...
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https://lup.lub.lu.s...
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https://doi.org/10.1...
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Abstract
Ämnesord
Stäng
- 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.
Ämnesord
- NATURVETENSKAP -- Kemi -- Fysikalisk kemi (hsv//swe)
- NATURAL SCIENCES -- Chemical Sciences -- Physical Chemistry (hsv//eng)
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