Atomistic Models from Orientation and Distance Constraints Using EPR of a Bifunctional Spin Label.

ABSTRACT: We have used high-resolution orientation and distance measurements derived from electron paramagnetic resonance of a bifunctional spin label (BSL) to build and refine atomistic models of protein structure. We demonstrate this approach by investigating the effects of nucleotide binding on the structure of myosin's catalytic domain while myosin is in complex with actin. Constraints for orientation of individual helices were obtained in a previous study from continuous-wave electron paramagnetic resonance of myosin labeled at specific sites with BSLs in oriented muscle fibers. In this study, new distance constraints were derived from double electron-electron resonance on myosin constructs labeled with a BSL specifically at two sites. Using these complementary constraints together, we thorough

SUBMITTER: Binder BP 

PROVIDER: S-EPMC6702148 | biostudies-literature | 2019 Jul

REPOSITORIES: biostudies-literature