Robust structure-based resonance assignment for functional protein studies by NMR.

ABSTRACT: High-throughput functional protein NMR studies, like protein interactions or dynamics, require an automated approach for the assignment of the protein backbone. With the availability of a growing number of protein 3D structures, a new class of automated approaches, called structure-based assignment, has been developed quite recently. Structure-based approaches use primarily NMR input data that are not based on J-coupling and for which connections between residues are not limited by through bonds magnetization transfer efficiency. We present here a robust structure-based assignment approach using mainly H(N)-H(N) NOEs networks, as well as (1)H-(15) N residual dipolar couplings and chemical shifts. The NOEnet complete search algorithm is robust against assignment errors, even for sparse inpu

SUBMITTER: Stratmann D 

PROVIDER: S-EPMC2813526 | biostudies-literature | 2010 Feb

REPOSITORIES: biostudies-literature