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Strategie NMR wyznaczania struktur białek w roztworze

Ejchart A.

Wiadomości Chemiczne

2005

[Z] 59, 1-2

23--45

A number of reasons have hindered the use of NMR spectroscopy as a tool for the protein structure determination. Recently, the advance in the NMR equipment, spectral techniques and isotope labelling has resulted in an enormous growth of NMR-determined protein structures. After a brief presentation of protein structure and conformation several types of NMR-derived constraints and the characteristic features of chemical shifts in proteins are discussed. Short-range, distance and dihedral angle constraints are valuable, but cumulative errors can appear when succesive constraints are used to determine spatial relationship of remote parts of a protein. Therefore, long-range constraints derived from residual dipolar couplings are highly complementary to the short-range constraints. Modern strategies to the NMR-based protein structure determination depend on the size of studied biomolecules. Small proteins (Mcz< 10 kDa) can be studied with the use of two-dimensional (2D) 1H NMR techniques. Medium size proteins (Mcz < 30 kDa) require double isotopic labeling 15N/13C and multidimensional (3D and 4D) heteronuclear techniques. There is no well established strategy to the structure determination of large proteins (Mcz > 30 kDa) yet. The most promising approaches take advantage of triple isotopic labeling 15N/13C/2H and the transverse relaxation optimized spectroscopy (TROSY), both resulting in the reduction of signal width.