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Significance Allostery is a common strategy used by nature to transmit information in proteins, including membrane signaling systems, wherein binding of one ligand affects avidity for binding another ligand in a distal site. Methods are needed for elucidation of functional groups that are critical for coupling between the binding sites, which we call allosteric participants. Identifying and characterizing allosteric participants is important for understanding the allosteric mechanism and crucial for developing new drugs. We develop an NMR method to detect allosteric participants that relies on their multistate nature, and we apply this method to a membrane protein, the potassium channel KcsA. We confirm the importance of specific amino acid side chains for allostery through analysis of binding affinities.

Identifying coupled clusters of allostery participants through chemical shift perturbations