Phys.org August 23, 2023
In nature, proteins that switch between two conformations in response to environmental stimuli structurally transduce biochemical information in a manner analogous to how transistors control information flow in computing devices. Designing proteins with two distinct but fully structured conformations is a challenge for protein design as it requires sculpting an energy landscape with two distinct minima. A team of researchers in the US (University of Washington, Lawrence Berkeley National Laboratory, University of Milwaukee) described the design of “hinge” proteins that populate one designed state in the absence of ligand and a second designed state in the presence of ligand. X-ray crystallography, electron microscopy, double electron-electron resonance spectroscopy, and binding measurements demonstrated that despite the significant structural differences the two states were designed with atomic level accuracy and that the conformational and binding equilibria were closely coupled… read more. TECHNICAL ARTICLE
Diversity of hinge structures and conformational changes… Credit: SCIENCE, 17 Aug 2023, Vol 381, Issue 6659, pp. 754-760