Modulating protein alignment in a liquid-crystalline medium through conservative mutagenesis

Residual dipolar couplings (RDCs) readily can be measured for molecules aligned in a magnetic field and carry a wealth of information on both molecular structure and internal dynamics.1,2 Introduction of suitable alignment media, mostly lyotropic liquid crystals, but also anisotropically compressed hydrogels,3,4 have enabled accurate NMR measurement of RDCs in isotopically enriched proteins, where they are becoming increasingly used to evaluate and/or refine structural quality and to probe interna