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Title: Resolving biomolecular motion and interactions by R₂ and R₁ρ relaxation dispersion NMR
Authors: Walinda, Erik
Morimoto, Daichi  kyouindb  KAKEN_id  orcid (unconfirmed)
Sugase, Kenji  kyouindb  KAKEN_id  orcid (unconfirmed)
Author's alias: 森本, 大智
菅瀬, 謙治
Keywords: NMR spectroscopy
Protein dynamics
DNA/RNA dynamics
Chemical exchange
Conformational exchange
Biomolecular interactions
Relaxation dispersion
Issue Date: 15-Sep-2018
Publisher: Elsevier BV
Journal title: Methods
Volume: 148
Start page: 28
End page: 38
Abstract: Among the tools of structural biology, NMR spectroscopy is unique in that it not only derives a static three-dimensional structure, but also provides an atomic-level description of the local fluctuations and global dynamics around this static structure. A battery of NMR experiments is now available to probe the motions of proteins and nucleic acids over the whole biologically relevant timescale from picoseconds to hours. Here we focus on one of these methods, relaxation dispersion, which resolves dynamics on the micro- to millisecond timescale. Key biological processes that occur on this timescale include enzymatic catalysis, ligand binding, and local folding. In other words, relaxation-dispersion-resolved dynamics are often closely related to the function of the molecule and therefore highly interesting to the structural biochemist. With an astounding sensitivity of ∼0.5%, the method detects low-population excited states that are invisible to any other biophysical method. The kinetics of the exchange between the ground state and excited states are quantified in the form of the underlying exchange rate, while structural information about the invisible excited state is obtained in the form of its chemical shift. Lastly, the population of the excited state can be derived. This diversity in the information that can be obtained makes relaxation dispersion an excellent method to study the detailed mechanisms of conformational transitions and molecular interactions. Here we describe the two branches of relaxation dispersion, R₂ and R₁ρ, discussing their applicability, similarities, and differences, as well as recent developments in pulse sequence design and data processing.
Rights: © 2018. This manuscript version is made available under the CC-BY-NC-ND 4.0 license
The full-text file will be made open to the public on 15 September 2019 in accordance with publisher's 'Terms and Conditions for Self-Archiving'.
This is not the published version. Please cite only the published version. この論文は出版社版でありません。引用の際には出版社版をご確認ご利用ください。
DOI(Published Version): 10.1016/j.ymeth.2018.04.026
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