The measurement of relaxation rates of degenerate ¹H transitions in methyl groups of proteins using acute angle radiofrequency pulses.

ABSTRACT: A simple NMR experiment for the measurement of transverse relaxation rates of degenerate ¹H spins in ¹³CH₃ methyl groups of deuterated proteins, is described. The experiment relies on the use of acute-angle ¹H radio-frequency pulses, whereby a series of methyl ¹H R₂ decays is acquired with different values of the ¹H pulse flip-angle, which modulates the relative contributions of the slow- and fast-relaxing components of ¹H magnetization during the relaxation delay. These are subsequently analyzed simultaneously to extract the transverse relaxation rates of both components (R_S and R_F), along with the rate of cross-relaxation between these components, δ. The dipolar ¹H-

SUBMITTER: Tugarinov V 

PROVIDER: S-EPMC8405580 | biostudies-literature | 2021 Sep

REPOSITORIES: biostudies-literature