An automated iterative approach for protein structure refinement using pseudocontact shifts.

ABSTRACT: NMR structure calculation using NOE-derived distance restraints requires a considerable number of assignments of both backbone and sidechains resonances, often difficult or impossible to get for large or complex proteins. Pseudocontact shifts (PCSs) also play a well-established role in NMR protein structure calculation, usually to augment existing structural, mostly NOE-derived, information. Existing refinement protocols using PCSs usually either require a sizeable number of sidechain assignments or are complemented by other experimental restraints. Here, we present an automated iterative procedure to perform backbone protein structure refinements requiring only a limited amount of backbone amide PCSs. Already known structural features from a starting homology model, in this case modules o

SUBMITTER: Cucuzza S 

PROVIDER: S-EPMC8473369 | biostudies-literature | 2021 Sep

REPOSITORIES: biostudies-literature