RDC derived protein backbone resonance assignment using fragment assembly.

ABSTRACT: Experimental residual dipolar couplings (RDCs) in combination with structural models have the potential for accelerating the protein backbone resonance assignment process because RDCs can be measured accurately and interpreted quantitatively. However, this application has been limited due to the need for very high-resolution structural templates. Here, we introduce a new approach to resonance assignment based on optimal agreement between the experimental and calculated RDCs from a structural template that contains all assignable residues. To overcome the inherent computational complexity of such a global search, we have adopted an efficient two-stage search algorithm and included connectivity data from conventional assignment experiments. In the first stage, a list of strings of resonances

SUBMITTER: Wang X 

PROVIDER: S-EPMC6936109 | biostudies-literature | 2011 Feb

REPOSITORIES: biostudies-literature