Nonlinear elasticity, proteinquakes, and the energy landscapes of functional transitions in proteins.

ABSTRACT: Large-scale motions of biomolecules involve linear elastic deformations along low-frequency normal modes, but for function nonlinearity is essential. In addition, unlike macroscopic machines, biological machines can locally break and then reassemble during function. We present a model for global structural transformations, such as allostery, that involve large-scale motion and possible partial unfolding, illustrating the method with the conformational transition of adenylate kinase. Structural deformation between open and closed states occurs via low-frequency modes on separate reactant and product surfaces, switching from one state to the other when energetically favorable. The switching model is the most straightforward anharmonic interpolation, which allows the barrier for a process to

SUBMITTER: Miyashita O 

PROVIDER: S-EPMC240658 | biostudies-literature | 2003 Oct

REPOSITORIES: biostudies-literature