Premium
A novel approach for assesing macromolecular complexes combining soft‐docking calculations with NMR data
Author(s) -
Morelli Xavier J.,
Palma P. Nuno,
Guerlesquin Françoise,
Rigby Alan C.
Publication year - 2001
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1110/ps.07501
Subject(s) - docking (animal) , heteronuclear single quantum coherence spectroscopy , heteronuclear molecule , searching the conformational space for docking , nuclear magnetic resonance spectroscopy , macromolecule , chemistry , computational chemistry , ab initio , biological system , protein structure , stereochemistry , biochemistry , biology , organic chemistry , medicine , nursing
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.