The acquisition of standard NMR spectra takes from a few minutes (1D spectra) to 3/4 days (3D or 4D spectra) for each experiment. A full set of experiments for protein structure determination usually ...

NMR spectroscopy has gained acceptance in the last few decades as a powerful technology for protein structure determination, but it is limited to small (<40 kDa), stable, soluble proteins that do ...

Still, getting enough protein is a far cry from a crystal or NMR spectroscopy structure. “For a long time people thought that the main problem was expression levels, and if you could express ...

Structure determination by NMR typically requires a protein concentration of 0.5 mM or greater, stable for several days at the desired temperature, usually 20-40 o C. Proteins and peptides should be ...

Nuclear magnetic resonance (NMR) spectroscopy allows scientists to probe an intrinsically disordered protein’s structure and dynamics as it wiggles around in solution. NMR spectrometers use strong ...

It has the capability of providing detailed information about structure and dynamics of molecules as well as how atoms are connected to each other. NMR can identify different nuclei in a molecule and ...

Accurate protein structure prediction is critical for decoding ... nuclear magnetic resonance (NMR), and cryo-electron ...

This work includes using in cell NMR, a technique to study the structure and dynamics of proteins within living cells. I currently study intrinsically disordered proteins using solution NMR. Proteins ...

The new 1.2 GHz NMR complements the existing 800 MHz NMR in Basel and other high-field NMRs for protein structure determination, measurement of protein dynamics, ligand binding studies ...

An international team of scientists, including University of Groningen Professor of Solid State NMR Spectroscopy ... ‘Knowing the structure of the protein clump is a critical piece of the ...