Nuclear magnetic resonance (NMR) spectroscopy can be used to monitor the dynamic behavior of a protein at a multitude of specific sites. Moreover, protein movements on a broad range of timescales ...
Finally, a summary of methods for relating NMR derived motional parameters to ... A deep insight into the function of proteins will only be obtained through a combined study of both structural ...
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 ...
Solution NMR data on peptides can be acquired at concentrations > 0.1mM for a 1D or to get structural information >1-2mM in aqueous buffers with 10% D 2 O. Phosphate buffer is an economical ...
Professor Hough currently studies intrinsically disordered proteins using solution NMR. Proteins containing disordered domains perform many important cellular functions. The aggregations of this ...
NMR can identify different nuclei in a molecule and analyze large proteins and other large molecules using three dimensional (3-D) techniques. This instrument provides powerful information for the ...
I currently study intrinsically disordered proteins using solution NMR. Proteins containing disordered domains perform many important cellular functions. The aggregations of some members of this ...
1) NMR data was used to the structure determination and 2) interaction site mapping and 3) all data was used to construct a model of the complex. Disclaimer: AAAS and EurekAlert! are not ...
and is particularly beneficial for multi-dimensional experiments in biomolecular NMR, where time savings up to a factor of 4 in 3D experiments or 10 and even more in 4D and 5D experiments can be ...