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High‐Dimensional NMR Spectra for Structural Studies of Biomolecules
Author(s) -
Kazimierczuk Krzysztof,
Stanek Jan,
ZawadzkaKazimierczuk Anna,
Koźmiński Wiktor
Publication year - 2013
Publication title -
chemphyschem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.016
H-Index - 140
eISSN - 1439-7641
pISSN - 1439-4235
DOI - 10.1002/cphc.201300277
Subject(s) - biomolecule , nmr spectra database , spectral line , nuclear magnetic resonance spectroscopy , chemistry , materials science , chemical physics , nuclear magnetic resonance , computational chemistry , nanotechnology , physics , stereochemistry , astronomy
Recent developments in the acquisition and processing of NMR data sets facilitate the recording of ultra‐high‐resolution NMR spectra in a reasonable time. The new experiments allow easy resonance assignment for folded and unfolded proteins, as well as the precise determination of spectral parameters, for example, chemical shifts, NOE contacts, coupling constants or cross‐correlated relaxation rates. Owing to exceptional resolution of 4D–6D spectroscopy, detailed studies of biomolecules of unprecedented complexity are now possible. Herein, the principles of acquisition and processing methods are presented. The main applications of high‐dimensional NMR experiments, including backbone and side‐chain resonance assignment in proteins, as well as heteronuclear edited NOE techniques are reviewed.