Fast evaluation of protein dynamics from deficient 15N relaxation data

Handle URI:
http://hdl.handle.net/10754/627505
Title:
Fast evaluation of protein dynamics from deficient 15N relaxation data
Authors:
Jaremko, Łukasz; Jaremko, Mariusz; Ejchart, Andrzej; Nowakowski, Michał ( 0000-0002-1356-0301 )
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.
KAUST Department:
Biological and Environmental Sciences and Engineering (BESE) Division; Bioscience Program
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.
Publisher:
Springer Nature
Journal:
Journal of Biomolecular NMR
Issue Date:
28-Mar-2018
DOI:
10.1007/s10858-018-0176-3
Type:
Article
ISSN:
0925-2738; 1573-5001
Sponsors:
The research by LJ and MJ reported in this publication was supported by funding from King Abdullah University of Science and Technology (KAUST).
Additional Links:
http://link.springer.com/article/10.1007/s10858-018-0176-3
Appears in Collections:
Articles; Bioscience Program; Biological and Environmental Sciences and Engineering (BESE) Division

Full metadata record

DC FieldValue Language
dc.contributor.authorJaremko, Łukaszen
dc.contributor.authorJaremko, Mariuszen
dc.contributor.authorEjchart, Andrzejen
dc.contributor.authorNowakowski, Michałen
dc.date.accessioned2018-04-16T11:27:42Z-
dc.date.available2018-04-16T11:27:42Z-
dc.date.issued2018-03-28en
dc.identifier.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.en
dc.identifier.issn0925-2738en
dc.identifier.issn1573-5001en
dc.identifier.doi10.1007/s10858-018-0176-3en
dc.identifier.urihttp://hdl.handle.net/10754/627505-
dc.description.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.en
dc.description.sponsorshipThe research by LJ and MJ reported in this publication was supported by funding from King Abdullah University of Science and Technology (KAUST).en
dc.publisherSpringer Natureen
dc.relation.urlhttp://link.springer.com/article/10.1007/s10858-018-0176-3en
dc.rightsThis article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made.en
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/en
dc.subject15N magnetic relaxationen
dc.subjectModel-free approachen
dc.subjectProtein dynamicsen
dc.subjectRatio, product, and difference of relaxation ratesen
dc.subjectSemi-quantitative analysis of 15N relaxation dataen
dc.titleFast evaluation of protein dynamics from deficient 15N relaxation dataen
dc.typeArticleen
dc.contributor.departmentBiological and Environmental Sciences and Engineering (BESE) Divisionen
dc.contributor.departmentBioscience Programen
dc.identifier.journalJournal of Biomolecular NMRen
dc.eprint.versionPublisher's Version/PDFen
dc.contributor.institutionInstitute of Biochemistry and Biophysics, Polish Academy of Science, Pawinskiego 5A, Warszawa, 02-106, , , Polanden
dc.contributor.institutionFaculty of Chemistry, Biological and Chemical Research Centre, University of Warsaw, Żwirki i Wigury 101, Warszawa, 02-089, , , Polanden
kaust.authorJaremko, Łukaszen
kaust.authorJaremko, Mariuszen
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