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Measurement of13Cα-13CO cross-relaxation rates in15N-/13C-labelled proteins

✍ Scribed by Florence Cordier; Bernhard Brutscher; Dominique Marion

Publisher
Springer Netherlands
Year
1996
Tongue
English
Weight
616 KB
Volume
7
Category
Article
ISSN
0925-2738

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✦ Synopsis

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 13C0-13C ~ 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 15N-/~3C-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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