Fast evaluation of protein dynamics from deficient 15N relaxation data

Abstract
Simple and convenient method of protein dynamics evaluation from the insufficient experimental N relaxation data is presented basing on the ratios, products, and differences of longitudinal and transverse 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 and R, can be elucidated. The generalized order parameter, S, describes motions on the time scale faster than the overall tumbling correlation time (pico- to nanoseconds), while the chemical exchange term, R, identifies processes slower than the overall tumbling correlation time (micro- to milliseconds). Advantages and disadvantages of different methods of data handling are thoroughly discussed.

Citation
Jaremko Ł, Jaremko M, Ejchart A, Nowakowski M (2018) Fast evaluation of protein dynamics from deficient 15N relaxation data. Journal of Biomolecular NMR. Available: http://dx.doi.org/10.1007/s10858-018-0176-3.

Acknowledgements
The research by LJ and MJ reported in this publication was supported by funding from King Abdullah University of Science and Technology (KAUST).

Publisher
Springer Nature

Journal
Journal of Biomolecular NMR

DOI
10.1007/s10858-018-0176-3

PubMed ID
29594733

Additional Links
http://link.springer.com/article/10.1007/s10858-018-0176-3

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