Protein structure determination and refinement with raw NMR data

Chad Rienstra, University of Illinois at Urbana-Champaign

Usage Details

NMR is an extremely powerful technique for investigating protein structure, dynamics and interactions. However, standard methods for NMR-based protein structure determination and chemical shift assignment require time-consuming data collection and extensive manual analysis efforts. We have recently presented a qualitatively distinct and novel approach, called Comparative, Objective Measurement of Protein Architectures by Scoring Shifts (COMPASS), that determines the structure of a protein solely by numerical comparison of structural models (derived from homology modeling and/or molecular dynamics) with a single, unanalyzed 2D 13C- 13C NMR spectrum. The current COMPASS implementation relies on selecting the correct structure from a candidate pool, relying primarily on homology modeling and low-computational-cost refinement strategies. The aim of this proposed project is to extend this approach to the screening and refinement of structures produced through a metadynamics approach using the COMPASS scoring function as a biasing potential.