Fast evaluation of protein dynamics from deficient 15N relaxation data
KAUST DepartmentBiological and Environmental Sciences and Engineering (BESE) Division
Online Publication Date2018-03-28
Print Publication Date2018-04
Permanent link to this recordhttp://hdl.handle.net/10754/627505
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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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- Sampling of protein dynamics in nanosecond time scale by 15N NMR relaxation and self-diffusion measurements.
- Authors: Orekhov VY, Korzhnev DM, Pervushin KV, Hoffmann E, Arseniev AS
- Issue date: 1999 Aug
- A comprehensive analysis of multifield 15N relaxation parameters in proteins: determination of 15N chemical shift anisotropies.
- Authors: Canet D, Barthe P, Mutzenhardt P, Roumestand C
- Issue date: 2001 May 16
- Recent developments in (15)N NMR relaxation studies that probe protein backbone dynamics.
- Authors: Ishima R
- Issue date: 2012
- Detection of nano-second internal motion and determination of overall tumbling times independent of the time scale of internal motion in proteins from NMR relaxation data.
- Authors: Larsson G, Martinez G, Schleucher J, Wijmenga SS
- Issue date: 2003 Dec
- A new spin probe of protein dynamics: nitrogen relaxation in 15N-2H amide groups.
- Authors: Xu J, Millet O, Kay LE, Skrynnikov NR
- Issue date: 2005 Mar 9