Characterizing GPCR Allostery by NMR Spectroscopy

NMR Methods to Study Dynamic Allostery

Nuclear magnetic resonance (NMR) spectroscopy provides a unique toolbox of experimental probes for studying dynamic processes on a wide range of timescales, ranging from picoseconds to milliseconds and beyond. Along with NMR hardware developments, recent methodological advancements have enabled the characterization of allosteric proteins at unprecedented detail, revealing intriguing aspects of ...

Unravelling Glycobiology by NMR Spectroscopy

Extended para-hydrogenation monitored by NMR spectroscopy.

A system that provides a sustained hyperpolarized (1)H NMR signal in an aqueous medium is reported. The enhanced signal lasts much longer than typical (1)H T(1) values, uncovering new possibilities for implementing hyperpolarized (1)H NMR/MRI experiments or performing kinetics studies that would not otherwise be detectable.

Millisecond protein folding studied by NMR spectroscopy.

Proteins are involved in virtually every biological process and in order to function, it is necessary for these polypeptide chains to fold into the unique, native conformation. This folding process can take place rapidly. NMR line shape analyses and transverse relaxation measurements allow protein folding studies on a microsecond-to-millisecond time scale. Together with an overview of current a...

Protein complexes studied by NMR spectroscopy.

Recent advances in NMR methods now allow protein complexes to be studied in great detail in a wide range of solution conditions. Isotope-enrichment strategies, resonance-assignment approaches and structural-determination methods have evolved to the point where almost any type of complex involving proteins of reasonable size may be studied in a straightforward way. A variety of isotope editing a...