Direct 13C-detection for carbonyl relaxation studies of protein dynamics
Author:
Publisher
Elsevier BV
Subject
Condensed Matter Physics,Nuclear and High Energy Physics,Biochemistry,Biophysics
Reference42 articles.
1. Backbone dynamics of proteins as studied by nitrogen-15 inverse detected heteronuclear NMR spectroscopy: application to staphylococcal nuclease
2. NMR relaxation and protein mobility
3. Carbonyl Carbon Probe of Local Mobility in 13C,15N-Enriched Proteins Using High-Resolution Nuclear Magnetic Resonance
4. Study of protein dynamics in solution by measurement of 13C?-13CO NOE and 13CO longitudinal relaxation
5. Temperature dependence of protein backbone motion from carbonyl 13C and amide 15N NMR relaxation
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1. Intrinsically disordered proteins studied by NMR spectroscopy;Journal of Magnetic Resonance Open;2024-03
2. 13C Direct Detected NMR for Challenging Systems;Chemical Reviews;2022-01-13
3. Enzyme–Substrate–Cofactor Dynamical Networks Revealed by High-Resolution Field Cycling Relaxometry;Biochemistry;2020-06-01
4. Time-Resolved Protein Side-Chain Motions Unraveled by High-Resolution Relaxometry and Molecular Dynamics Simulations;Journal of the American Chemical Society;2018-09-07
5. The Use of 13C Direct-Detect NMR to Characterize Flexible and Disordered Proteins;Methods in Enzymology;2018
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