NMR Methods to Study the Dynamics of SH2 Domain–Phosphopeptide Complexes

Publikation: Beitrag in Buch/Bericht/Sammelwerk/Konferenzband › Beitrag in Buch/Sammelwerk › Forschung › Peer-Review

Autorschaft

  • Michelangelo Marasco
  • John P. Kirkpatrick
  • Vittoria Nanna
  • Teresa Carlomagno

Organisationseinheiten

Externe Organisationen

  • Memorial Sloan-Kettering Cancer Center
  • University of Birmingham
Forschungs-netzwerk anzeigen

Details

OriginalspracheEnglisch
Titel des SammelwerksSH2 Domains
UntertitelFunctional Modules and Evolving Tools in Biology
ErscheinungsortNew York
Seiten25-37
Seitenumfang13
Auflage1.
ISBN (elektronisch)978-1-0716-3393-9
PublikationsstatusVeröffentlicht - 6 Sept. 2023

Publikationsreihe

NameMethods in Molecular Biology
Band2705
ISSN (Print)1064-3745
ISSN (elektronisch)1940-6029

Abstract

Nuclear magnetic resonance (NMR) spectroscopy is the method of choice for studying the dynamics of biological macromolecules in solution. By exploiting the intricate interplay between the effects of protein motion (both overall rotational diffusion and internal mobility) and nuclear spin relaxation, NMR allows molecular motion to be probed at atomic resolution over a wide range of timescales, including picosecond (bond vibrations and methyl-group rotations), nanosecond (loop motions and rotational diffusion), and microsecond–millisecond (ligand binding, allostery). In this chapter, we describe different NMR pulse schemes (R1, R1ρ, heteronuclear NOE, and CPMG relaxation dispersion) to characterize the dynamics of SH2 domains. As an example, we use the N-SH2 domain of protein tyrosine phosphatase SHP2 in complex with two phosphopeptides derived from immune checkpoint receptor PD-1 (ITIM and ITSM).

ASJC Scopus Sachgebiete

  • Biochemie, Genetik und Molekularbiologie (insg.)
  • Molekularbiologie
  • Biochemie, Genetik und Molekularbiologie (insg.)
  • Genetik

Zitieren

NMR Methods to Study the Dynamics of SH2 Domain–Phosphopeptide Complexes. / Marasco, Michelangelo; Kirkpatrick, John P.; Nanna, Vittoria et al.
SH2 Domains: Functional Modules and Evolving Tools in Biology. 1. Aufl. New York, 2023. S. 25-37 (Methods in Molecular Biology; Band 2705).

Publikation: Beitrag in Buch/Bericht/Sammelwerk/Konferenzband › Beitrag in Buch/Sammelwerk › Forschung › Peer-Review

Marasco, M, Kirkpatrick, JP, Nanna, V & Carlomagno, T 2023, NMR Methods to Study the Dynamics of SH2 Domain–Phosphopeptide Complexes. in SH2 Domains: Functional Modules and Evolving Tools in Biology. 1. Aufl., Methods in Molecular Biology, Bd. 2705, New York, S. 25-37. https://doi.org/10.1007/978-1-0716-3393-9_2
Marasco, M., Kirkpatrick, J. P., Nanna, V., & Carlomagno, T. (2023). NMR Methods to Study the Dynamics of SH2 Domain–Phosphopeptide Complexes. In SH2 Domains: Functional Modules and Evolving Tools in Biology (1. Aufl., S. 25-37). (Methods in Molecular Biology; Band 2705).. https://doi.org/10.1007/978-1-0716-3393-9_2
Marasco M, Kirkpatrick JP, Nanna V, Carlomagno T. NMR Methods to Study the Dynamics of SH2 Domain–Phosphopeptide Complexes. in SH2 Domains: Functional Modules and Evolving Tools in Biology. 1. Aufl. New York. 2023. S. 25-37. (Methods in Molecular Biology). doi: 10.1007/978-1-0716-3393-9_2
Marasco, Michelangelo ; Kirkpatrick, John P. ; Nanna, Vittoria et al. / NMR Methods to Study the Dynamics of SH2 Domain–Phosphopeptide Complexes. SH2 Domains: Functional Modules and Evolving Tools in Biology. 1. Aufl. New York, 2023. S. 25-37 (Methods in Molecular Biology).
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