Evolution of the structure and dynamics of bovine serum albumin induced by thermal denaturation

Matsarskaia, Olga (författare): Institut Laue-Langevin, 71 Avenue des Martyrs, 38042 Grenoble, France

Bühl, Lena (författare): Institut Laue-Langevin, 71 Avenue des Martyrs, Grenoble, 38042, France; Institut für Angewandte Physik, Auf der Morgenstelle 10, Tübingen, 72076, Germany,University of Tübingen

Beck, Christian (författare): Institut Laue-Langevin, 71 Avenue des Martyrs, Grenoble, 38042, France; Institut für Angewandte Physik, Auf der Morgenstelle 10, Tübingen, 72076, Germany,University of Tübingen

Grimaldo, Marco (författare): Institut Laue-Langevin, 71 Avenue des Martyrs, Grenoble, 38042, France

Schweins, Ralf (författare): Institut Laue-Langevin, 71 Avenue des Martyrs, Grenoble, 38042, France

Zhang, Fajun (författare): Institut für Angewandte Physik, Auf der Morgenstelle 10, Tübingen, 72076, Germany,University of Tübingen

Seydel, Tilo (författare): Institut Laue-Langevin, 71 Avenue des Martyrs, Grenoble, 38042, France

Schreiber, Frank (författare): Institut für Angewandte Physik, Auf der Morgenstelle 10, Tübingen, 72076, Germany,University of Tübingen

Roosen-Runge, Felix (författare): Malmö University,Lund University,Lunds universitet,Malmö universitet,Institutionen för biomedicinsk vetenskap (BMV),Biofilms Research Center for Biointerfaces,Division of Physical Chemistry, Lund University, Naturvetarvägen 14, Lund, 22100, Sweden,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

(creator_code:org_t)

2020
2020
Engelska.
Ingår i: Physical Chemistry, Chemical Physics - PCCP. - : Royal Society of Chemistry. - 1463-9076 .- 1463-9084. ; 22, s. 18507-18517

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Abstract Ämnesord

Stäng

Protein denaturation in concentrated solutions consists of the unfolding of the native protein structure, and subsequent cross-linking into clusters or gel networks. While the kinetic evolution of structure has been studied for some cases, the underlying microscopic dynamics of proteins has so far been neglected. However, protein dynamics is essential to understand the specific nature of assembly processes, such as diffusion-limited growth, or vitrification of dense liquids. Here, we present a study on thermal denaturation of concentrated solutions of bovine serum albumin (BSA) in D2O with and without NaCl. Using small-angle scattering, we provide information on structure before, during and after denaturation. Using quasi-elastic neutron scattering, we monitor in real-time the microscopic dynamics and dynamical confinement throughout the entire denaturation process covering protein unfolding and cross-linking. After denaturation, the protein dynamics is slowed down in salty solutions compared to those in pure water, while the stability and dynamics of the native solution appears unaffected by salt. The approach presented here opens opportunities to link microscopic dynamics to emerging structural properties, with implications for assembly processes in soft and biological matter.

Av författaren/redakt...: Matsarskaia, Olg ...; Bühl, Lena; Beck, Christian; Grimaldo, Marco; Schweins, Ralf; Zhang, Fajun; visa fler...; Seydel, Tilo; Schreiber, Frank; Roosen-Runge, Fe ...; visa färre...

Om ämnet

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