Incorporating the BEST methodology in experiments for measuring paramagnetic relaxation enhancements

Anthis NJ, Clore GM (2013) Sequence-specific determination of protein and peptide concentrations by absorbance at 205 nm. Protein Sci 22:851–858

Article  Google Scholar 

Anthis NJ, Clore GM (2015) Visualizing transient dark states by NMR spectroscopy. Q Rev Biophys 48:35–116

Article  Google Scholar 

Bieri M, d’Auvergne EJ, Gooley PR (2011) Relaxgui: a new software for fast and simple NMR relaxation data analysis and calculation of ps-ns and μs motion of proteins. J Biomol NMR 50:147–155

Article  Google Scholar 

Clore GM (2015) Practical aspects of paramagnetic relaxation enhancement in biological macromolecules. Methods Enzymol 564:485–497

Article  Google Scholar 

Clore GM, Iwahara J (2009) Theory, practice, and applications of paramagnetic relaxation enhancement for the characterization of transient low-population states of biological macromolecules and their complexes. Chem Rev 109:4108–4139

Article  Google Scholar 

Davis SM, Romig BL, Abe AA, Loening NM (2025) An improved variant of tobacco etch virus (TEV) protease that does not need reducing agents. Protein Sci 34:e70049

Article  Google Scholar 

Di Nicola A et al (2025) Investigating binding between dynein intermediate chain and dynactin p150Glued. Protein Sci. Publ. Protein Soc, TBD

Google Scholar 

Donaldson LW et al (2001) Structural characterization of proteins with an attached ATCUN motif by paramagnetic relaxation enhancement NMR spectroscopy. J Am Chem Soc 123:9843–9847

Article  ADS  Google Scholar 

Farjon J et al (2009) Longitudinal-relaxation-enhanced NMR experiments for the study of nucleic acids in solution. J Am Chem Soc 131:8571–8577

Article  ADS  Google Scholar 

Favier A, Brutscher B (2011) Recovering lost magnetization: polarization enhancement in biomolecular NMR. J Biomol NMR 49:9–15

Article  Google Scholar 

Iwahara J, Tang C, Clore GM (2007) Practical aspects of 1H transverse paramagnetic relaxation enhancement measurements on macromolecules. J Magn Reson 184:185–195

Article  ADS  Google Scholar 

Jansson M et al (1996) High-level production of uniformly 15N- and 13C-enriched fusion proteins in Escherichia coli. J Biomol NMR 7:131–141

Article  Google Scholar 

Jensen MR, Ruigrok RWH, Blackledge M (2013) Describing intrinsically disordered proteins at atomic resolution by NMR. Curr Opin Struct Biol 23:426–435

Article  Google Scholar 

Kay LE, Keifer P, Saarinen T (1992) Pure absorption gradient enhanced heteronuclear single quantum correlation spectroscopy with improved sensitivity. J Am Chem Soc 114:10663–10665

Article  ADS  Google Scholar 

Kosol S, Contreras-Martos S, Cedeño C, Tompa P (2013) Structural characterization of intrinsically disordered proteins by NMR spectroscopy. Molecules 18:10802–10828

Article  Google Scholar 

Lescop E, Schanda P, Brutscher B (2007) A set of BEST triple-resonance experiments for time-optimized protein resonance assignment. J Magn Reson 187(1):163–169

Article  ADS  Google Scholar 

Lescop E, Kern T, Brutscher B (2010) Guidelines for the use of band-selective radiofrequency pulses in hetero-nuclear NMR: example of longitudinal-relaxation-enhanced BEST-type 1H-15N correlation experiments. J Magn Reson San Diego Calif 1997 203:190–198

Google Scholar 

Loening NM, Jara KA, Barbar EJ (2025) NMR approaches to identify transient structure and interactions of intrinsically disordered dynein intermediate chain. J Mol Biol. https://doi.org/10.1016/j.jmb.2025.169380

Article  Google Scholar 

Meiboom S, Gill D (1958) Modified spin-echo method for measuring nuclear relaxation times. Rev Sci Instrum 29:688–691

Article  ADS  Google Scholar 

Meissner A, Schulte-Herbrüggen T, Briand J, Sørensen OW (1998) Double spin-state-selective coherence transfer. Application for two-dimensional selection of multiplet components with long transverse relaxation times. Mol Phys 95:1137–1142

ADS  Google Scholar 

Palmer AG, Cavanagh J, Wright PE, Rance M (1991) Sensitivity improvement in proton-detected two-dimensional heteronuclear correlation NMR spectroscopy. J Magn Resonance (1969) 93(1):151–170

Article  Google Scholar 

Pervushin K, Riek R, Wider G, Wüthrich K (1998) Transverse relaxation-optimized spectroscopy (TROSY) for NMR studies of aromatic spin systems in 13C-labeled proteins. J Am Chem Soc 120:6394–6400

Article  ADS  Google Scholar 

Pervushin K, Vögeli B, Eletsky A (2002) Longitudinal 1H relaxation optimization in TROSY NMR spectroscopy. J Am Chem Soc 124:12898–12902

Article  ADS  Google Scholar 

Schanda P, Brutscher B (2005) Very fast two-dimensional NMR spectroscopy for real-time investigation of dynamic events in proteins on the time scale of seconds. J Am Chem Soc 127:8014–8015

Article  ADS  Google Scholar 

Schanda P, Kupce E, Brutscher B (2005) Sofast-HMQC experiments for recording two-dimensional heteronuclear correlation spectra of proteins within a few seconds. J Biomol NMR 33:199–211

Article  Google Scholar 

Schanda P, Van Melckebeke H, Brutscher B (2006) Speeding up three-dimensional protein NMR experiments to a few minutes. J Am Chem Soc 128:9042–9043

Article  ADS  Google Scholar 

Skinner SP et al (2016) Ccpnmr analysisassign: a flexible platform for integrated NMR analysis. J Biomol NMR 66:111–124

Article  Google Scholar 

Vranken WF et al (2005) The CCPN data model for NMR spectroscopy: development of a software pipeline. Proteins 59:687–696

Article  Google Scholar 

Comments (0)

No login
gif