Very fast two-dimensional NMR spectroscopy for real-time investigation of dynamic events in proteins on the time scale of seconds.
We demonstrate for different protein samples that 2D 1H-15N correlation NMR spectra can be recorded in a few seconds of acquisition time using a new band-selective optimized flip-angle short-transient heteronuclear multiple quantum coherence experiment. This has enabled us to measure fast hydrogen-deuterium exchange rate constants along the backbone of a small globular protein fragment by real-time 2D NMR.
Schanda
Paul
P
Institut de Biologie Structurale Jean-Pierre Ebel CNRS-CEA-UJF, 41 rue Jules Horowitz, 38027 Grenoble, France.
Brutscher
Bernhard
B
D041961:Deuterium Exchange Measurement; D007700:Kinetics; D008024:Ligands; D008958:Models, Molecular; D009587:Nitrogen Isotopes; D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods*; D010088:Oxidoreductases / Q000737:chemistry*; D010446:Peptide Fragments / Q000737:chemistry*; D043367:Ralstonia / Q000201:enzymology
D008024:Ligands; D009587:Nitrogen Isotopes; D010446:Peptide Fragments; D010088:Oxidoreductases; C021551:mercuric reductase