Production of a Specifically Labeled Protein in mg Quantities for NMR Analysis

2003 
The structural and functional analysis of proteins via NMR methodologies is gaining more and more attention [1,2] because interactions (e.g, drug-screening) can be studied in much more detail and technical breakthrough like the new cryoprobe allows the use of significantly lower protein concentrations, thus reducing the aggregation problem due to low protein solubility. However, NMR is ususally limited to relatively low-molecular-weight proteins (<40 kDa) and requires extensive isotope labeling of the protein using special and costly expression procedures. In addition, it takes several months to a year to determine a high-resolution structure of a protein using standard methodology, mainly because many peaks overlap, so that time-consuming manual assignment work is necessary.
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