Computational study for protein-protein docking using global optimization and empirical potentials.

ABSTRACT: Protein-protein interactions are important for biochemical processes in biological systems. The 3D structure of the macromolecular complex resulting from the protein-protein association is a very useful source to understand its specific functions. This work focuses on computational study for protein-protein docking, where the individually crystallized structures of interacting proteins are treated as rigid, and the conformational space generated by the two interacting proteins is explored extensively. The energy function consists of intermolecular electrostatic potential, desolvation free energy represented by empirical contact potential, and simple repulsive energy terms. The conformational space is six dimensional, represented by translational vectors and rotational angles formed between

SUBMITTER: Lee K 

PROVIDER: S-EPMC2635596 | biostudies-literature | 2008 Jan

REPOSITORIES: biostudies-literature