High‐Dimensional NMR Spectra for Structural Studies of Biomolecules. Issue 13 (21st June 2013)

• Record Type: Journal Article
• Authors: Kazimierczuk, Krzysztof; Stanek, Jan; Zawadzka‐Kazimierczuk, Anna; Koźmiński, Wiktor
• Is Part Of: Chemphyschem. Volume 14:Issue 13(2013)
• Page Start: 3015
• Page End: 3025
• Publication Date: 2013-06-21
• Subjects: Chemistry, Physical and theoretical -- Periodicals; 541.05
• DOI: 10.1002/cphc.201300277
• Languages: English
• ISSNs: 1439-4235

Abstract

<abstract abstract-type="main" xml:lang="en"> <title>Abstract</title> <p>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.</p> </abstract>