The utility of acute (< 90°) angle 1H radio-frequency (RF) pulses for a number of NMR applications targeting 13CH3 methyl groups in selectively 13CH3-labeled, deuterated proteins is described. We show first that sensitive and efficient selection of 1H and 13C transitions belonging to the I = 1/2 manifolds of 13CH3 groups, can be achieved with 1H RF pulses adjusted to ~42°, effectively reducing the 13CH3(AX3) spin-system to its simpler 13C-1H(A-X) counterparts. The use of ‘magic’-angle (54.7º) 1H pulses, is shown to simplify and improve the sensitivity of methyl 1H relaxation rate measurements for small-to-medium sized proteins. Further, we demonstrate that the transfer of magnetization to and from the slow-relaxing 13C transitions of 13CH3 methyl groups can be optimized by careful adjustment of the angles of 1H pulses in INEPT-based transfer schemes. Examples of experiments for characterization of fast (picosecond time-scale) dynamics of methyl-bearing side-chains that rely on the separation of groups of 13C magnetization modes using a variety of acute angle 1H pulses, are provided. We also describe a simple NMR experiment for the measurement of transverse relaxation rates of degenerate 1H transitions in 13CH3 methyl groups, where a series of methyl 1H R2 decays is acquired with different values of 1H pulse flip-angles that achieves modulation of the relative contributions of the slow- and fast-relaxing components of 1H magnetization during the relaxation delay. Special emphasis is given to the utility of acute angle 1H pulses for characterization of chemical exchange on the micro-to-millisecond time-scale in degenerate spin-systems by Carr-Purcell-Meiboom-Gill (CPMG) relaxation dispersion NMR experiments - a ‘steady-state’ methyl 1H CPMG scheme, where acute-angle 1H radiofrequency pulses are applied after each CPMG spin-echo in-phase with methyl 1H magnetization, resulting in establishment of a ‘steady-state’ for effective rates of magnetization decay.