THz time scale structural rearrangements and binding modes in lysozyme-ligand interactions.

ABSTRACT: Predicting the conformational changes in proteins that are relevant for substrate binding is an ongoing challenge in the aim of elucidating the functional states of proteins. The motions that are induced by protein-ligand interactions are governed by the protein global modes. Our measurements indicate that the detected changes in the global backbone motion of the enzyme upon binding reflect a shift from the large-scale collective dominant mode in the unbound state towards a functional twisting deformation that assists in closing the binding cleft. Correlated motion in lysozyme has been implicated in enzyme function in previous studies, but detailed characterization of the internal fluctuations that enable the protein to explore the ensemble of conformations that ultimately foster large-sca

SUBMITTER: Woods KN 

PROVIDER: S-EPMC4049381 | biostudies-literature | 2014 Mar

REPOSITORIES: biostudies-literature