Damry et al. evaluates the impact of individual substitutions in primary sequence of a globular protein on its conformational dynamics. They demonstrate that only two mutations in core residues of a streptococcal protein (Gβ1) variant can synergistically create conformational exchange, one destabilizing the native structure while the other allowing two new conformational states to be accessed on the energy landscape.
- Adam M. Damry
- Marc M. Mayer
- Roberto A. Chica
