Engineering the entropy-driven free-energy landscape of a dynamic nanoporous protein assembly.

ABSTRACT: De novo design and construction of stimuli-responsive protein assemblies that predictably switch between discrete conformational states remains an essential but highly challenging goal in biomolecular design. We previously reported synthetic, two-dimensional protein lattices self-assembled via disulfide bonding interactions, which endows them with a unique capacity to undergo coherent conformational changes without losing crystalline order. Here, we carried out all-atom molecular dynamics simulations to map the free-energy landscape of these lattices, validated this landscape through extensive structural characterization by electron microscopy and established that it is predominantly governed by solvent reorganization entropy. Subsequent redesign of the protein surface with conditionally r

SUBMITTER: Alberstein R 

PROVIDER: S-EPMC6056010 | biostudies-literature | 2018 Jul

REPOSITORIES: biostudies-literature