A hybrid method that combines sparse NMR spectroscopy data with evolutionary residue-residue coupling information is used to solve accurate structures of large proteins.

Protein NMR spectroscopy provides an important complement to X-ray crystallography for structural genomics, both for determining three-dimensional protein structures and in characterizing their ...

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 ...

A pressure of 3,000 bar is applied to the cold shock protein B of Bacillus subtilis in a small tube in the NMR spectroscopy laboratory at the University of Konstanz. This is roughly three times ...

More information: Si Yan et al. Atomic-resolution structure of the CAP-Gly domain of dynactin on polymeric microtubules determined by magic angle spinning NMR spectroscopy, Proceedings of the ...

This article outlines some of the newly developed NMR techniques for detecting amino acid residues such as proline in Intrinsically Disordered Proteins (IDPs).

Héctor holds a PhD in biochemistry from the Rocasolano Institute for Physical Chemistry where he studied the structure, dynamics and interactions of peptides and proteins using NMR spectroscopy.

The NMR techniques they used were lifetime line broadening, Carr-Purcell-Meinboom-Gill (CPMG) relaxation dispersion spectroscopy, and exchange-induced chemical shifts.

NMR spectroscopy is especially well-suited for the study of intrinsically disordered proteins (IDPs) and intrinsically disordered regions (IDRs) which are in general highly flexible and do not have a ...

Through the use of the nuclear magnetic resonance (NMR) spectroscopy, Kalodimos and his co-workers were able to determine how proteins slide along the lengthy strands forming the helix structure ...