Site-directed mutagenesis nuclear magnetic resonance

Meiering EM, Li H, Delcamp TJ, et al. Contributions of tryptophan 24 and glutamate 30 to binding long-lived water molecules in the ternary complex of human dihydrofolate reductase with methotrexate and NADPH studies by site directed mutagenesis and nuclear magnetic resonance spectroscopy. J Mol Biol 1995 241 309-325. 

The three-dimensional structures of several ribonucleases have been determined by single-crystal X-ray diffraction methods and recently also by nuclear magnetic resonance (NMR) spectroscopy. For a number of RNases, several crystal structure analyses have been performed. In these crystal structures, different inhibitors, substrate analogs, or reaction products have been used, different protein variants generated by site-directed mutagenesis have been present, or different crystal forms of the same enzyme have been studied. 

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