Fast evaluation of protein dynamics from deficient ¹⁵N relaxation data.

ABSTRACT: Simple and convenient method of protein dynamics evaluation from the insufficient experimental ¹⁵N relaxation data is presented basing on the ratios, products, and differences of longitudinal and transverse ¹⁵N 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, S² and R _ex , can be elucidated. The generalized order parameter, S², describes motions on the time scale faster than the overall tumbling correlation time (pico- to nanoseconds), while the chemical exchange term, R _ex ,

SUBMITTER: Jaremko L 

PROVIDER: S-EPMC5953972 | biostudies-literature | 2018 Apr

REPOSITORIES: biostudies-literature