Protein NMR Spectroscopy
2006; Linguagem: Inglês
10.1002/3527600906.mcb.200500055
Autores Tópico(s)Protein Structure and Dynamics
ResumoNuclear magnetic resonance (NMR) spectroscopy provides unique information about protein structure, dynamics, hydration, and folding in aqueous solution, and has become a pivotal biophysical technique to investigate biological macromolecules. Although the first application of NMR spectroscopy to study proteins date back to the 1960s, its widespread use for proteins was fostered only in the late 1970s and early 1980s by introduction of two-dimensional NMR spectroscopy conducted on spectrometers equipped with superconducting high-field magnets. Advances made in the subsequent 25 years until today have established NMR as an indispensable tool to study even large proteins with molecular masses above 100 kDa. These advances were due to new approaches for efficient production of stable isotope labeled proteins, novel spin relaxation, optimized and rapid sampling of NMR data collection strategies, and the advent of highly sensitive cryogenic probes used for signal detection at field strengths corresponding to 500–900 MHz proton resonance frequency. Recently, the outstanding value of NMR was demonstrated for high-throughput structure determination in the newly emerging field of structural genomics, which makes protein NMR spectroscopy also a key tool for systems biology.
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