University of Oulu

J. Phys. Chem. B 2019, 123, 39, 8178–8185,

A quasielastic neutron scattering investigation on the molecular self-dynamics of human myelin protein P2

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Author: Laulumaa, Saara1,2; Koza, Michael Marek3; Seydel, Tilo3;
Organizations: 1Faculty of Biochemistry and Molecular Medicine and Biocenter Oulu, University of Oulu, Oulu, Finland
2European Spallation Source, Lund, Sweden
3Institut Laue-Langevin, Grenoble, France
4Department of Biomedicine, University of Bergen, Bergen, Norway
5CNR-IOM, OGG, Grenoble, France
Format: article
Version: accepted version
Access: open
Online Access: PDF Full Text (PDF, 2.8 MB)
Persistent link:
Language: English
Published: American Chemical Society, 2019
Publish Date: 2021-03-04


The human myelin protein P2 is a membrane binding protein believed to maintain correct lipid composition and organization in peripheral nerve myelin. Its function is related to its ability to stack membranes, and this function can be enhanced by the P38G mutation, whereby the overall protein structure does not change but the molecular dynamics increase. Mutations in P2 are linked to human peripheral neuropathy. Here, the dynamics of wild-type P2 and the P38G variant were studied using quasielastic neutron scattering on time scales from 10 ps to 1 ns at 300 K. The results suggest that the mutant protein dynamics are increased on both the fastest and the slowest measured time scales, by increasing the dynamics amplitude and/or the portion of atoms participating in the movement.

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Series: The journal of physical chemistry. B
ISSN: 1520-6106
ISSN-E: 1520-5207
ISSN-L: 1520-5207
Volume: 123
Issue: 39
Pages: 8178 - 8185
DOI: 10.1021/acs.jpcb.9b05320
Type of Publication: A1 Journal article – refereed
Field of Science: 1182 Biochemistry, cell and molecular biology
Funding: This work was financially supported by the European Spallation Source, the Academy of Finland, the Emil Aaltonen Foundation (Finland), and the Sigrid Jusélius Foundation (Finland).
Copyright information: This document is the Accepted Manuscript version of a Published Work that appeared in final form in The Journal of Physical Chemistry B, copyright © American Chemical Society after peer review and technical editing by the publisher. To access the final edited and published work see