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I. Zhukov, A. Ejchart

NMR spectroscopy in structural proteomics. NMR-based protein structure

determination (in English)

Polimery 2003, No 1, 28


DOI: dx.doi.org/10.14314/polimery.2003.028


Summary

The pros and cons of NMR spectroscopy as a tool for the protein structure determination are discussed. Recently, the advance in the NMR equipment, spectral techniques and isotope labelling resulted in an enormous growth of NMR-determined protein structures. Modern approaches to the NMR-based protein structure determinations are based on several types of experimentally derived constraints. Short-range, distance and dihedral angle constraints are valuable, but cumulative errors can appear when successive constraints are used to determine spatial relationship of remote parts of a protein. Therefore, long-range constraints derived from residual dipolar couplings and nuclear relaxation data of anisotropically tumbling molecules are highly complementary to the short-range constraints.


Keywords: NMR spectroscopy, protein structure in solution, NMR structural constraints


I. Zhukov, A. Ejchart

PolNMR spectroscopy in structural proteomics. NMR-based protein structure determination (in English)