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Simple and convenient method of protein dynamics evaluation from the insufficient experimental 15 N relaxation data is presented basing on the ratios, products, and differences of longitudinal and transverse 15 N relaxation rates obtained at a single magnetic field. Firstly, the proposed approach allows evaluating overall tumbling correlation time (nanosecond time scale). Next, local parameters of the model-free approach characterizing local mobility of backbone amide N-H vectors on two different time scales, S 2 and R ex , can be elucidated. The generalized order parameter, S 2 , describes motions on the time scale faster than the overall tumbling correlation time (pico- to nanoseconds), while the chemical exchange term, R ex , identifies processes slower than the overall tumbling correlation time (micro- to milliseconds). Advantages and disadvantages of different methods of data handling are thoroughly discussed.

Fast evaluation of protein dynamics from deficient 15N relaxation data