@inbook{d5ff48c2bfd940d9924ec5b4b248d0ed,
title = "BCL-2 Protein Family Interaction Analysis by Nuclear Magnetic Resonance Spectroscopy",
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.",
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)",
author = "Garner, {Thomas P.} and Evripidis Gavathiotis",
note = "Publisher Copyright: {\textcopyright} 2019, Springer Science+Business Media, LLC, part of Springer Nature.",
year = "2019",
doi = "10.1007/978-1-4939-8861-7_15",
language = "English (US)",
series = "Methods in Molecular Biology",
publisher = "Humana Press Inc.",
pages = "217--231",
booktitle = "Methods in Molecular Biology",
}