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

Research output: Chapter in book/report/conference proceeding › Contribution to book/anthology › Research › peer review

Authors

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

Research Organisations

External Research Organisations

  • Memorial Sloan-Kettering Cancer Center
  • University of Birmingham
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Details

Original languageEnglish
Title of host publicationMethods in Molecular Biology
Pages25-37
Number of pages13
Publication statusPublished - 2023

Publication series

NameMethods in Molecular Biology
Volume2705
ISSN (Print)1064-3745
ISSN (electronic)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).

Keywords

    Allostery, Chemical exchange, Nuclear magnetic resonance (NMR) spectroscopy, Phosphopeptides, Protein dynamics, Spin relaxation, Src-homology 2 (SH2) domain

ASJC Scopus subject areas

Cite this

NMR Methods to Study the Dynamics of SH2 Domain–Phosphopeptide Complexes. / Marasco, Michelangelo; Kirkpatrick, John P.; Nanna, Vittoria et al.
Methods in Molecular Biology. 2023. p. 25-37 (Methods in Molecular Biology; Vol. 2705).

Research output: Chapter in book/report/conference proceeding › Contribution to book/anthology › Research › peer review

Marasco, M, Kirkpatrick, JP, Nanna, V & Carlomagno, T 2023, NMR Methods to Study the Dynamics of SH2 Domain–Phosphopeptide Complexes. in Methods in Molecular Biology. Methods in Molecular Biology, vol. 2705, pp. 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 Methods in Molecular Biology (pp. 25-37). (Methods in Molecular Biology; Vol. 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 Methods in Molecular Biology. 2023. p. 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. Methods in Molecular Biology. 2023. pp. 25-37 (Methods in Molecular Biology).
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