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Fast evaluation of protein dynamics from deficient 15N relaxation data

Jaremko, Łukasz and Jaremko, Mariusz and Ejchart, Andrzej and Nowakowski, Michał (2018) Fast evaluation of protein dynamics from deficient 15N relaxation data. Journal of Biomolecular NMR, 70 (4). pp. 219-228. ISSN 0925-2738

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Official URL: https://link.springer.com/article/10.1007/s10858-0...

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 Rex, 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, Rex, identifies processes slower than the overall tumbling correlation time (micro- to milliseconds). Advantages and disadvantages of different methods of data handling are thoroughly discussed.

Item Type:Article
Subjects:Q Science > QD Chemistry
Divisions:Laboratory of Biological NMR
ID Code:1563
Deposited By: professor Andrzej Ejchart
Deposited On:27 Jun 2018 07:50
Last Modified:27 Jun 2018 07:50

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