Diffusivelike Motions in a Solvent-Free Protein-Polymer Hybrid

Giorgio  Schirò; Alex P. S.  Brogan; et al.

doi:10.1103/PhysRevLett.126.088102

Diffusivelike Motions in a Solvent-Free Protein-Polymer Hybrid

Giorgio Schirò, Alex P. S. Brogan, et al.

Research output: Contribution to journal › Book/Film/Article review (Academic Journal) › peer-review

7 Citations (Scopus)

140 Downloads (Pure)

Abstract

The interaction between proteins and hydration water stabilizes protein structure and promotes functional dynamics, with water translational motions enabling protein flexibility. Engineered solvent-free protein-polymer hybrids have been shown to preserve protein structure, function, and dynamics. Here, we used neutron scattering, protein and polymer perdeuteration, and molecular dynamics simulations to explore how a polymer dynamically replaces water. Even though relaxation rates and vibrational properties are strongly modified in polymer coated compared to hydrated proteins, liquidlike polymer dynamics appear to plasticize the conjugated protein in a qualitatively similar way as do hydration-water translational motions.

Original language	English
Article number	088102
Number of pages	7
Journal	Physical Review Letters
Volume	126
Issue number	8
DOIs	https://doi.org/10.1103/PhysRevLett.126.088102
Publication status	Published - 26 Feb 2021

Bibliographical note

Funding Information:
We are indebted to Laurent Heux for the use of calorimeter at CERMAV (Grenoble) and Pierre Sailler for the assistance during the calorimetry experiment. We thank Matthias Heyden for providing his custom-made trajectory analysis software. Financial support by the CEA, the CNRS, and the U. G. A. is acknowledged, as well as a grant from the Agence Nationale de la Recherche (Project No. ANR-11-BSV5-027) to M. W. The I. B. S. acknowledges integration into the Interdisciplinary Research Institute of Grenoble (IRIG, CEA). This work used the platforms of the Grenoble Instruct-ERIC center (ISBG ; UMS 3518 CNRS-CEA-UGA-EMBL) within the Grenoble Partnership for Structural Biology (PSB), supported by FRISBI (ANR-10-INBS-0005-02) and GRAL, financed within the University Grenoble Alpes graduate school (Ecoles Universitaires de Recherche) CBH-EUR-GS (ANR-17-EURE-0003). This project has received funding from the European Union’s 7th Framework Programme for research, technological development and demonstration under the NMI3-II Grant No. 283883. We thank the UKRI for support for AWP (MR/S016430/1 and EP/K026720/1).

Publisher Copyright:
© 2021 American Physical Society.

Access to Document

10.1103/PhysRevLett.126.088102

Full-text PDF (final published version)
This is the final published version of the article (version of record). It first appeared online via American Physical Society at https://doi.org/10.1103/PhysRevLett.126.088102 . Please refer to any applicable terms of use of the publisher.
Final published version, 608 KB

Handle.net

Persistent link

Embargoed Document

Full-text PDF (author’s accepted manuscript)
Accepted author manuscript, 725 KB
Request copy

Embargoed Document

Supplementary information PDF
Accepted author manuscript, 1.24 MB
Request copy

HPC (High Performance Computing) and HTC (High Throughput Computing) Facilities
Alam, S. R. (Manager), Williams, D. A. G. (Manager), Eccleston, P. E. (Manager) & Greene, D. (Manager)
Facility/equipment: Facility

Cite this

@article{b9995fb29563458b898b3e83cc780125,

title = "Diffusivelike Motions in a Solvent-Free Protein-Polymer Hybrid",

abstract = "The interaction between proteins and hydration water stabilizes protein structure and promotes functional dynamics, with water translational motions enabling protein flexibility. Engineered solvent-free protein-polymer hybrids have been shown to preserve protein structure, function, and dynamics. Here, we used neutron scattering, protein and polymer perdeuteration, and molecular dynamics simulations to explore how a polymer dynamically replaces water. Even though relaxation rates and vibrational properties are strongly modified in polymer coated compared to hydrated proteins, liquidlike polymer dynamics appear to plasticize the conjugated protein in a qualitatively similar way as do hydration-water translational motions.",

author = "Giorgio Schir{\`o} and Brogan, {Alex P. S.} and Sessions, {Richard B} and Perriman, {Adam W} and {et al.}",

note = "Funding Information: We are indebted to Laurent Heux for the use of calorimeter at CERMAV (Grenoble) and Pierre Sailler for the assistance during the calorimetry experiment. We thank Matthias Heyden for providing his custom-made trajectory analysis software. Financial support by the CEA, the CNRS, and the U. G. A. is acknowledged, as well as a grant from the Agence Nationale de la Recherche (Project No. ANR-11-BSV5-027) to M. W. The I. B. S. acknowledges integration into the Interdisciplinary Research Institute of Grenoble (IRIG, CEA). This work used the platforms of the Grenoble Instruct-ERIC center (ISBG ; UMS 3518 CNRS-CEA-UGA-EMBL) within the Grenoble Partnership for Structural Biology (PSB), supported by FRISBI (ANR-10-INBS-0005-02) and GRAL, financed within the University Grenoble Alpes graduate school (Ecoles Universitaires de Recherche) CBH-EUR-GS (ANR-17-EURE-0003). This project has received funding from the European Union{\textquoteright}s 7th Framework Programme for research, technological development and demonstration under the NMI3-II Grant No. 283883. We thank the UKRI for support for AWP (MR/S016430/1 and EP/K026720/1). Publisher Copyright: {\textcopyright} 2021 American Physical Society.",

year = "2021",

month = feb,

day = "26",

doi = "10.1103/PhysRevLett.126.088102",

language = "English",

volume = "126",

journal = "Physical Review Letters",

issn = "0031-9007",

publisher = "American Physical Society (APS)",

number = "8",

}

TY - JOUR

T1 - Diffusivelike Motions in a Solvent-Free Protein-Polymer Hybrid

AU - Schirò, Giorgio

AU - Brogan, Alex P. S.

AU - Sessions, Richard B

AU - Perriman, Adam W

AU - et al.

N1 - Funding Information: We are indebted to Laurent Heux for the use of calorimeter at CERMAV (Grenoble) and Pierre Sailler for the assistance during the calorimetry experiment. We thank Matthias Heyden for providing his custom-made trajectory analysis software. Financial support by the CEA, the CNRS, and the U. G. A. is acknowledged, as well as a grant from the Agence Nationale de la Recherche (Project No. ANR-11-BSV5-027) to M. W. The I. B. S. acknowledges integration into the Interdisciplinary Research Institute of Grenoble (IRIG, CEA). This work used the platforms of the Grenoble Instruct-ERIC center (ISBG ; UMS 3518 CNRS-CEA-UGA-EMBL) within the Grenoble Partnership for Structural Biology (PSB), supported by FRISBI (ANR-10-INBS-0005-02) and GRAL, financed within the University Grenoble Alpes graduate school (Ecoles Universitaires de Recherche) CBH-EUR-GS (ANR-17-EURE-0003). This project has received funding from the European Union’s 7th Framework Programme for research, technological development and demonstration under the NMI3-II Grant No. 283883. We thank the UKRI for support for AWP (MR/S016430/1 and EP/K026720/1). Publisher Copyright: © 2021 American Physical Society.

PY - 2021/2/26

Y1 - 2021/2/26

N2 - The interaction between proteins and hydration water stabilizes protein structure and promotes functional dynamics, with water translational motions enabling protein flexibility. Engineered solvent-free protein-polymer hybrids have been shown to preserve protein structure, function, and dynamics. Here, we used neutron scattering, protein and polymer perdeuteration, and molecular dynamics simulations to explore how a polymer dynamically replaces water. Even though relaxation rates and vibrational properties are strongly modified in polymer coated compared to hydrated proteins, liquidlike polymer dynamics appear to plasticize the conjugated protein in a qualitatively similar way as do hydration-water translational motions.

AB - The interaction between proteins and hydration water stabilizes protein structure and promotes functional dynamics, with water translational motions enabling protein flexibility. Engineered solvent-free protein-polymer hybrids have been shown to preserve protein structure, function, and dynamics. Here, we used neutron scattering, protein and polymer perdeuteration, and molecular dynamics simulations to explore how a polymer dynamically replaces water. Even though relaxation rates and vibrational properties are strongly modified in polymer coated compared to hydrated proteins, liquidlike polymer dynamics appear to plasticize the conjugated protein in a qualitatively similar way as do hydration-water translational motions.

U2 - 10.1103/PhysRevLett.126.088102

DO - 10.1103/PhysRevLett.126.088102

M3 - Book/Film/Article review (Academic Journal)

C2 - 33709739

SN - 0031-9007

VL - 126

JO - Physical Review Letters

JF - Physical Review Letters

IS - 8

M1 - 088102

ER -

Diffusivelike Motions in a Solvent-Free Protein-Polymer Hybrid

Abstract

Bibliographical note

Access to Document

Handle.net

Embargoed Document

Embargoed Document

Fingerprint

Equipment

HPC (High Performance Computing) and HTC (High Throughput Computing) Facilities

Cite this