Język Polski
English
Published
: 2022-09-17
NMR spectroscopy in structural proteomics. NMR-based protein structure determination
Abstract
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.
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Zasady cytowania
Zhukow, I., & Ejchart, A. (2022). NMR spectroscopy in structural proteomics. NMR-based protein structure determination. Polimery, 48(1), 28–34. Retrieved from https://ichp.vot.pl/index.php/p/article/view/1833
