Cookies on this website

We use cookies to ensure that we give you the best experience on our website. If you click 'Accept all cookies' we'll assume that you are happy to receive all cookies and you won't see this message again. If you click 'Reject all non-essential cookies' only necessary cookies providing core functionality such as security, network management, and accessibility will be enabled. Click 'Find out more' for information on how to change your cookie settings.

NMR methods are now able to give detailed structural, dynamic and electronic information about drugs and ligands while constrained at their site of action in membrane-embedded receptors, information which is essential for mechanistic descriptions of their action and design of new ligands. Using solid state NMR methods, a peptic ulcer drug analogue has been described at atomic resolution (to +/- 0.3 A between two atoms) at its site of action in the gastric H+/K+-ATPase, and the aromaticity of the agonist binding site of the nicotinic acetylcholine receptor has been demonstrated, with both targets in functionally competent membranes under conditions similar to those used in screening assays. G-protein-coupled receptor ligands and prosthetic groups are also being resolved using NMR methods.


Journal article


Curr Opin Biotechnol

Publication Date





48 - 53


Amino Acid Sequence, Anti-Ulcer Agents, Enzyme Inhibitors, GTP-Binding Proteins, H(+)-K(+)-Exchanging ATPase, Ligands, Magnetic Resonance Spectroscopy, Membrane Proteins, Models, Molecular, Molecular Sequence Data, Peptic Ulcer, Pharmaceutical Preparations, Proton Pump Inhibitors, Receptors, Cell Surface, Receptors, Nicotinic