Energy landscape and multiroute folding of topologically complex proteins adenylate kinase and 2ouf-knot.

ABSTRACT: While fast folding of small proteins has been relatively well characterized by experiments and theories, much less is known for slow folding of larger proteins, for which recent experiments suggested quite complex and rich folding behaviors. Here, we address how the energy landscape theory can be applied to these slow folding reactions. Combining the perfect-funnel approximation with a multiscale method, we first extended our previous atomic-interaction based coarse grained (AICG) model to take into account local flexibility of protein molecules. Using this model, we then investigated the energy landscapes and folding routes of two proteins with complex topologies: a multidomain protein adenylate kinase (AKE) and a knotted protein 2ouf-knot. In the AKE folding, consistent with experimental

SUBMITTER: Li W 

PROVIDER: S-EPMC3497823 | biostudies-literature | 2012 Oct

REPOSITORIES: biostudies-literature