Structural determination of biomolecular interfaces by nuclear magnetic resonance of proteins with reduced proton density.

ABSTRACT: Protein interactions are important for understanding many molecular mechanisms underlying cellular processes. So far, interfaces between interacting proteins have been characterized by NMR spectroscopy mostly by using chemical shift perturbations and cross-saturation via intermolecular cross-relaxation. Although powerful, these techniques cannot provide unambiguous estimates of intermolecular distances between interacting proteins. Here, we present an alternative approach, called REDSPRINT (REDduced/Standard PRoton density INTerface identification), to map protein interfaces with greater accuracy by using multiple NMR probes. Our approach is based on monitoring the cross-relaxation from a source protein (or from an arbitrary ligand that need not be a protein) with high proton density to a

SUBMITTER: Ferrage F 

PROVIDER: S-EPMC3637030 | biostudies-literature | 2010 May

REPOSITORIES: biostudies-literature