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The Onset of Molecule‐Spanning Dynamics in Heat Shock Protein Hsp90
Institute of Physical Chemistry University of Freiburg Albertstrasse 21 79104 Freiburg Germany.ORCID iD: 0000-0002-7103-3788
Institute of Applied Physics University of Tübingen Auf der Morgenstelle 10 72076 Tübingen Germany;Science Division Institut Max von Laue ‐ Paul Langevin 71 avenue des Martyrs Grenoble 38042 France.ORCID iD: 0000-0001-7214-3447
Institute of Physical Chemistry University of Freiburg Albertstrasse 21 79104 Freiburg Germany.ORCID iD: 0009-0001-5406-6086
Science Division Institut Max von Laue ‐ Paul Langevin 71 avenue des Martyrs Grenoble 38042 France.ORCID iD: 0000-0001-9630-1630
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2023 (English)In: Advanced Science, E-ISSN 2198-3844, Vol. 10, no 36Article in journal (Refereed) Published
Abstract [en]

Protein dynamics have been investigated on a wide range of time scales. Nano- and picosecond dynamics have been assigned to local fluctuations, while slower dynamics have been attributed to larger conformational changes. However, it is largely unknown how fast (local) fluctuations can lead to slow global (allosteric) changes. Here, fast molecule-spanning dynamics on the 100 to 200 ns time scale in the heat shock protein 90 (Hsp90) are shown. Global real-space movements are assigned to dynamic modes on this time scale, which is possible by a combination of single-molecule fluorescence, quasi-elastic neutron scattering and all-atom molecular dynamics (MD) simulations. The time scale of these dynamic modes depends on the conformational state of the Hsp90 dimer. In addition, the dynamic modes are affected to various degrees by Sba1, a co-chaperone of Hsp90, depending on the location within Hsp90, which is in very good agreement with MD simulations. Altogether, this data is best described by fast molecule-spanning dynamics, which precede larger conformational changes in Hsp90 and might be the molecular basis for allostery. This integrative approach provides comprehensive insights into molecule-spanning dynamics on the nanosecond time scale for a multi-domain protein.

Place, publisher, year, edition, pages
John Wiley & Sons, 2023. Vol. 10, no 36
Keywords [en]
heat shock protein 90, molecular dynamics simulations, neutron scattering, protein dynamics, single molecule fluorescence.
National Category
Biophysics
Identifiers
URN: urn:nbn:se:mau:diva-64145DOI: 10.1002/advs.202304262ISI: 001104702900001PubMedID: 37984887Scopus ID: 2-s2.0-85177222326OAI: oai:DiVA.org:mau-64145DiVA, id: diva2:1817550
Funder
German Research Foundation (DFG), 43194560German Research Foundation (DFG), 40322270German Research Foundation (DFG), INST 37/935‐1 FUGGAvailable from: 2023-12-06 Created: 2023-12-06 Last updated: 2024-01-04Bibliographically approved

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Roosen-Runge, Felix

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