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Updated: May 19, 2026

NMR 15N Relaxation Experiments for the Investigation of Picosecond to Nanoseconds Structural Dynamics of Proteins
Published on: November 1, 2024
Measurement of (13)C (α)- (13)CO cross-relaxation rates in (15)N-/ (13)C-labelled proteins
F Cordier1, B Brutscher, D Marion
1Institut de Biologie Structurale-Jean Pierre Ebel, C.E.A.-C.N.R.S., 41 Avenue des Martyrs, F-38027, Grenoble Cédex, France.
Abstract:
Internal motions play an important role in the biological function of proteins and NMR relaxation studies may characterize them over a wide range of frequencies. An experimental pulse scheme is proposed for the measurement of the (13)CO-(13)C(α) cross-relaxation rate. For sensitivity reasons, this measurement is performed in an indirect manner through several coherence transfer steps, which should thus be calibrated independently. Contributions of other relaxation pathways can be eliminated by the determination of the initial slope of the buildup curve. The cross-relaxation rates have been determined on a (15)N-/(13)C-labelled 116-residue protein and the significant variations along the sequence have been interpreted as evidence of an increased amount of fast local motion.
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