Fast evaluation of protein dynamics from deficient 15N relaxation data
KAUST DepartmentBiological and Environmental Sciences and Engineering (BESE) Division
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AbstractSimple 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.
CitationJaremko 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.
SponsorsThe research by LJ and MJ reported in this publication was supported by funding from King Abdullah University of Science and Technology (KAUST).
JournalJournal of Biomolecular NMR
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