Protein purification efforts for structural genomics will focus on automation for the readily-expressed proteins, and process development for the more difficult ones, such as membrane proteins.

We have used nuclear magnetic resonance (NMR) chemical shift perturbations in 2D 1 H-15 N heteronuclear single-quantum coherence (HSQC) spectra of 15 N-labeled proteins upon addition of ligands ...

NMR will undoubtedly play an essential role in investigating these protein types and exploiting their properties. References ‘Structure and Function of Intrinsically Disordered Proteins ...

Saying that, NMR has also been key to understanding the biological role, as well as the structure and dynamics of p53, so a number of articles on this protein have been published. NMR is unique in ...

This article discusses the use of NMR to investigate protein structure and dynamics in neurodegenerative diseases such as Alzheimer’s disease and Parkinson’s disease. ... Paramagnetic broadening in 2D ...

NMR can obtain highly precise data at every atom position that naturally contains or can be endowed with a magnetic isotope, like hydrogen-1, carbon-13, or nitrogen-15.

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

A University at Buffalo chemist has developed a new, high-throughput method for obtaining nuclear magnetic resonance (NMR) data that not only has the distinction of potentially performing orders of ...

Biophysicists in Germany and the US have used nuclear magnetic resonance to gain an important new insight into how proteins interact. The researchers were, for the first time, able to map out all the ...

An example of one MAS NMR spectrum. This is used to identify atoms in the molecule and, ultimately, for calculating their 3-D structures.

An NMR method enhanced by a very powerful amplifier, in combination with molecular dynamics simulation, now enables protein detection and accurate characterization at physiological concentrations.