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Updated: Feb 1, 2026

Examining BCL-2 Family Function with Large Unilamellar Vesicles
Published on: October 5, 2012
BCL-2 Protein Family Interaction Analysis by Nuclear Magnetic Resonance Spectroscopy
Thomas P Garner1,2,3,4, Evripidis Gavathiotis5,6,7,8
1Department of Biochemistry, Albert Einstein College of Medicine, Bronx, NY, USA.
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.
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