Distinct conformational changes occur within the intrinsically unstructured pro-domain of pro-Nerve Growth Factor in the presence of ATP and Mg2+

Paoletti, F, Covaceuszach, S, Cassetta, A et al. (6 more authors) (2023) Distinct conformational changes occur within the intrinsically unstructured pro-domain of pro-Nerve Growth Factor in the presence of ATP and Mg2+. Protein Science, 32 (2). e4563. ISSN 0961-8368

Abstract

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Authors/Creators:
Copyright, Publisher and Additional Information: © 2023 The Authors. Protein Science published by Wiley Periodicals LLC on behalf of The Protein Society. This is an open access article published under the terms of the Creative Commons Attribution License (CC-BY 4.0), which permits unrestricted use, distribution and reproduction in any medium, provided the original work is properly cited.
Keywords: conformational rearrangement of the Intrinsically Unstructured Domain (IUD), Hydrogen Deuterium eXchange-Mass Spectrometry (HDX-MS), intermolecular interactions, NMR spectroscopy, proNGF, Small Angle X-ray Scattering (SAXS)
Dates:
  • Accepted: 3 January 2023
  • Published (online): 5 January 2023
  • Published: February 2023
Institution: The University of Leeds
Academic Units: The University of Leeds > Faculty of Biological Sciences (Leeds) > School of Molecular and Cellular Biology (Leeds) > Biomolecular Mass Spectroscopy (Leeds)
Depositing User: Symplectic Publications
Date Deposited: 18 Jan 2023 11:58
Last Modified: 25 Jun 2023 23:13
Status: Published
Publisher: Wiley
Identification Number: https://doi.org/10.1002/pro.4563
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