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

Thomas P. Garner, Evripidis Gavathiotis

Research output: Chapter in Book/Report/Conference proceedingChapter


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.
Number of pages15
StatePublished - 2019

Publication series

NameMethods in Molecular Biology
ISSN (Print)1064-3745


  • 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


Dive into the research topics of 'BCL-2 Protein Family Interaction Analysis by Nuclear Magnetic Resonance Spectroscopy'. Together they form a unique fingerprint.

Cite this