Structural assembly of multidomain proteins and protein complexes guided by the overall rotational diffusion tensor.

ABSTRACT: We present a simple and robust approach that uses the overall rotational diffusion tensor as a structural constraint for domain positioning in multidomain proteins and protein-protein complexes. This method offers the possibility to use NMR relaxation data for detailed structure characterization of such systems provided the structures of individual domains are available. The proposed approach extends the concept of using long-range information contained in the overall rotational diffusion tensor. In contrast to the existing approaches, we use both the principal axes and principal values of protein's rotational diffusion tensor to determine not only the orientation but also the relative positioning of the individual domains in a protein. This is achieved by finding the domain arrangement in

SUBMITTER: Ryabov Y 

PROVIDER: S-EPMC2532536 | biostudies-literature | 2007 Jun

REPOSITORIES: biostudies-literature