Exploration of the dynamic properties of protein complexes predicted from spatially constrained protein-protein interaction networks.

ABSTRACT: Protein complexes are not static, but rather highly dynamic with subunits that undergo 1-dimensional diffusion with respect to each other. Interactions within protein complexes are modulated through regulatory inputs that alter interactions and introduce new components and deplete existing components through exchange. While it is clear that the structure and function of any given protein complex is coupled to its dynamical properties, it remains a challenge to predict the possible conformations that complexes can adopt. Protein-fragment Complementation Assays detect physical interactions between protein pairs constrained to ≤8 nm from each other in living cells. This method has been used to build networks composed of 1000s of pair-wise interactions. Significantly, these networks contain a

SUBMITTER: Yen EA 

PROVIDER: S-EPMC4038459 | biostudies-literature | 2014 May

REPOSITORIES: biostudies-literature