Fast evaluation of protein dynamics from deficient 15N relaxation data

Lukasz Jaremko, Mariusz Jaremko, Andrzej Ejchart, Michał Nowakowski

Research output: Contribution to journalArticlepeer-review

4 Scopus citations

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.
Original languageEnglish (US)
Pages (from-to)219-228
Number of pages10
JournalJournal of Biomolecular NMR
Volume70
Issue number4
DOIs
StatePublished - Mar 28 2018

Bibliographical note

KAUST Repository Item: Exported on 2020-10-01
Acknowledgements: The research by LJ and MJ reported in this publication was supported by funding from King Abdullah University of Science and Technology (KAUST).

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