The structure of the membrane anchor domain of the bacterial autotransporter YadA is solved by a solid-state NMR spectroscopy approach using a uniformly 13C- and 15N-labeled microcrystalline sample.

‘13C APSY-NMR for sequential assignment of intrinsically disordered proteins’ — Murrali MG, Schiavina M, Sainati V, Bermel W, Pierattelli R, Felli IC, Journal of Biomolecular NMR, 2018.

Proteins are central to many disciplines within the life sciences, not least protein-based pharmaceuticals. Changes in protein conformation, structure or interactions could have significant impact on ...

In particular, Dr. Rosenbaum and his laboratory use protein engineering, X-ray crystallography, and NMR spectroscopy to study the structure and dynamics of molecules involved in hormone signaling ...

Using nuclear magnetic resonance (NMR) spectroscopy, the researchers were able to determine how the structure of this protein changes as a drug-like molecule moves through it.

Another high-resolution method is nuclear magnetic resonance (NMR) spectroscopy, which can be used to characterize protein structure in liquids. However, this method is only practical when ...

Magic-angle-spinning NMR used to probe protein/microtubule assembly at atomic scale. by University of Delaware. An example of one MAS NMR spectrum. This is ...

Discover how vibration isolation enhances the accuracy and reliability of NMR spectroscopy by minimizing external ...

A strategy, based on solid-state NMR spectroscopy, for determining the structure of an oligomeric, seven-helix membrane protein (Anabaena sensory rhodopsin) in a lipid environment is described.