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dc.contributor.authorKharchenko, Vladlena
dc.contributor.authorNowakowski, Michal
dc.contributor.authorJaremko, Mariusz
dc.contributor.authorEjchart, Andrzej
dc.contributor.authorJaremko, Lukasz
dc.date.accessioned2020-09-13T05:25:57Z
dc.date.available2020-09-13T05:25:57Z
dc.date.issued2020-09-12
dc.date.submitted2020-05-01
dc.identifier.citationKharchenko, V., Nowakowski, M., Jaremko, M., Ejchart, A., & Jaremko, Ł. (2020). Dynamic 15N{1H} NOE measurements: a tool for studying protein dynamics. Journal of Biomolecular NMR. doi:10.1007/s10858-020-00346-6
dc.identifier.issn0925-2738
dc.identifier.issn1573-5001
dc.identifier.doi10.1007/s10858-020-00346-6
dc.identifier.urihttp://hdl.handle.net/10754/665074
dc.description.abstractAbstract Intramolecular motions in proteins are one of the important factors that determine their biological activity and interactions with molecules of biological importance. Magnetic relaxation of 15N amide nuclei allows one to monitor motions of protein backbone over a wide range of time scales. 15N{1H} nuclear Overhauser effect is essential for the identification of fast backbone motions in proteins. Therefore, exact measurements of NOE values and their accuracies are critical for determining the picosecond time scale of protein backbone. Measurement of dynamic NOE allows for the determination of NOE values and their probable errors defined by any sound criterion of nonlinear regression methods. The dynamic NOE measurements can be readily applied for non-deuterated or deuterated proteins in both HSQC and TROSY-type experiments. Comparison of the dynamic NOE method with commonly implied steady-state NOE is presented in measurements performed at three magnetic field strengths. It is also shown that improperly set NOE measurement cannot be restored with correction factors reported in the literature.
dc.description.sponsorshipThe authors would like to thank the Imaging and Characterization Core Lab at the King Abdullah University of Science and Technology (KAUST) for the access to the NMR facilities. This publication is based upon work supported by KAUST Office of Sponsored Research (OSR) under Award No. OSR-CRG2018-3792 (LJ) and through baseline-funds (LJ and MJ).
dc.publisherSpringer Nature
dc.relation.urlhttp://link.springer.com/10.1007/s10858-020-00346-6
dc.rightsThis article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder.
dc.rights.urihttps://creativecommons.org/licenses/by/4.0
dc.titleDynamic 15N{1H} NOE measurements: a tool for studying protein dynamics
dc.typeArticle
dc.contributor.departmentBiological and Environmental Sciences and Engineering (BESE) Division
dc.contributor.departmentBioscience
dc.contributor.departmentBioscience Program
dc.identifier.journalJournal of Biomolecular NMR
dc.eprint.versionPublisher's Version/PDF
dc.contributor.institutionFaculty of Chemistry, Biological and Chemical Research Centre, University of Warsaw, Żwirki i Wigury 101, 02-089, Warsaw, Poland.
dc.contributor.institutionInstitute of Biochemistry and Biophysics, Polish Academy of Sciences, Pawinskiego 5A, 02-106, Warsaw, Poland.
kaust.personKharchenko, Vladlena
kaust.personNowakowski, Michal
kaust.personJaremko, Mariusz
kaust.personJaremko, Lukasz
kaust.grant.numberOSR-CRG2018-3792
dc.date.accepted2020-08-12
refterms.dateFOA2020-09-13T05:27:13Z
kaust.acknowledged.supportUnitCharacterization Core Lab
kaust.acknowledged.supportUnitKAUST Office of Sponsored Research (OSR)


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This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder.
Except where otherwise noted, this item's license is described as This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder.