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

Michal K. Braun; Marco Grimaldo; Felix Roosen-Runge; Ingo Hoffmann; Orsolya Czakkel; Michael Sztucki; Fajun Zhang; Frank Schreiber; Tilo Seydel

doi:10.1021/acs.jpclett.7b00658

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

Michal K. Braun, Marco Grimaldo, Felix Roosen-Runge, Ingo Hoffmann, Orsolya Czakkel, Michael Sztucki, Fajun Zhang, Frank Schreiber, Tilo Seydel

Physical Chemistry

Research output: Contribution to journal › Article › peer-review

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 several nanoseconds. The presented analysis provides a general framework to access the structure and dynamics of macromolecular assemblies in solution.

Original language	English
Pages (from-to)	2590-2596
Number of pages	7
Journal	Journal of Physical Chemistry Letters
Volume	8
Issue number	12
DOIs	https://doi.org/10.1021/acs.jpclett.7b00658
Publication status	Published - 2017 Jun 15

Subject classification (UKÄ)

Physical Chemistry (including Surface- and Colloid Chemistry)

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10.1021/acs.jpclett.7b00658

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

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 several nanoseconds. The presented analysis provides a general framework to access the structure and dynamics of macromolecular assemblies in solution.",

author = "Braun, {Michal K.} and Marco Grimaldo and Felix Roosen-Runge and Ingo Hoffmann and Orsolya Czakkel and Michael Sztucki and Fajun Zhang and Frank Schreiber and Tilo Seydel",

year = "2017",

month = jun,

day = "15",

doi = "10.1021/acs.jpclett.7b00658",

language = "English",

volume = "8",

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journal = "Journal of Physical Chemistry Letters",

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TY - JOUR

T1 - Crowding-Controlled Cluster Size in Concentrated Aqueous Protein Solutions

T2 - Structure, Self- and Collective Diffusion

AU - Braun, Michal K.

AU - Grimaldo, Marco

AU - Roosen-Runge, Felix

AU - Hoffmann, Ingo

AU - Czakkel, Orsolya

AU - Sztucki, Michael

AU - Zhang, Fajun

AU - Schreiber, Frank

AU - Seydel, Tilo

PY - 2017/6/15

Y1 - 2017/6/15

N2 - 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.

AB - 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.

U2 - 10.1021/acs.jpclett.7b00658

DO - 10.1021/acs.jpclett.7b00658

M3 - Article

C2 - 28525282

AN - SCOPUS:85020824333

SN - 1948-7185

VL - 8

SP - 2590

EP - 2596

JO - Journal of Physical Chemistry Letters

JF - Journal of Physical Chemistry Letters

IS - 12

ER -

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

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