Journal
PROTEIN SCIENCE
Volume 10, Issue 10, Pages 2131-2137Publisher
COLD SPRING HARBOR LAB PRESS
DOI: 10.1110/ps.07501
Keywords
NMR; BiGGER; soft docking; protein complex; structure
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We present a novel and efficient approach for assessing protein-protein complex formation, which combines ab initio docking calculations performed with the protein docking algorithm BiGGER and chemical shift perturbation data collected with heteronuclear single quantum coherence (HSQC) or TROSY nuclear magnetic resonance (NMR) spectroscopy. This method, termed restrained soft-docking, is validated for several known protein complexes. These data demonstrate that restrained soft-docking extends the size limitations of NMR spectroscopy and provides an alternative method for investigating macromolecular protein complexes that requires less experimental time, effort, and resources. The potential utility of this novel NMR and simulated docking approach in current structural genomic initiatives is discussed.
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