BCL-2 Protein Family Interaction Analysis by Nuclear Magnetic Resonance Spectroscopy

Thomas P. Garner, Evripidis Gavathiotis

Research output: Chapter in Book/Report/Conference proceedingChapter

Abstract

Biomolecular nuclear magnetic resonance (NMR) is a powerful and versatile method for studying both protein–protein interactions (PPIs) and protein–small molecule binding. NMR has been used extensively in the investigation of BCL-2 family proteins revealing the structure of key family members, identifying binding partners and interaction sites, and screening small molecule modulators. In this chapter we discuss the application of NMR to identify interaction sites and structure determination of protein–protein and protein–small molecule complexes using two examples.

Original languageEnglish (US)
Title of host publicationMethods in Molecular Biology
PublisherHumana Press Inc.
Pages217-231
Number of pages15
DOIs
StatePublished - Jan 1 2019

Publication series

NameMethods in Molecular Biology
Volume1877
ISSN (Print)1064-3745

Keywords

  • BAX
  • BCL-2
  • BCL-2 family
  • Chemical shift perturbation (CSP)
  • MCL-1
  • Nuclear magnetic resonance (NMR)
  • Paramagnetic relaxation enhancement (PRE)
  • Protein–protein interactions (PPI)

ASJC Scopus subject areas

  • Molecular Biology
  • Genetics

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  • Cite this

    Garner, T. P., & Gavathiotis, E. (2019). BCL-2 Protein Family Interaction Analysis by Nuclear Magnetic Resonance Spectroscopy. In Methods in Molecular Biology (pp. 217-231). (Methods in Molecular Biology; Vol. 1877). Humana Press Inc.. https://doi.org/10.1007/978-1-4939-8861-7_15