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@article{2225678,
author = {Salvi, Nicola and Zapletal, Vojtěch and Jaseňáková, Zuzana and Zachrdla, Milan and Padrta, Petr and Narasimhan, Subhash and Marquardsen, Thorsten and Tyburn, JeanandMax and Žídek, Lukáš and Blackledge, Martin and Ferrage, Fabien and Kadeřávek, Pavel},
article_location = {UNITED STATES},
article_number = {20},
doi = {http://dx.doi.org/10.1016/j.bpj.2022.09.016},
keywords = {NMR; protein dynamics},
language = {eng},
issn = {0006-3495},
journal = {BIOPHYSICAL JOURNAL},
title = {Convergent views on disordered protein dynamics from NMR and computational approaches},
url = {https://linkinghub.elsevier.com/retrieve/pii/S0006-3495(22)00766-4},
volume = {121},
year = {2022}
}
TY - JOUR
ID - 2225678
AU - Salvi, Nicola - Zapletal, Vojtěch - Jaseňáková, Zuzana - Zachrdla, Milan - Padrta, Petr - Narasimhan, Subhash - Marquardsen, Thorsten - Tyburn, Jean-Max - Žídek, Lukáš - Blackledge, Martin - Ferrage, Fabien - Kadeřávek, Pavel
PY - 2022
TI - Convergent views on disordered protein dynamics from NMR and computational approaches
JF - BIOPHYSICAL JOURNAL
VL - 121
IS - 20
SP - 3785-3794
EP - 3785-3794
PB - CELL PRESS
SN - 00063495
KW - NMR
KW - protein dynamics
UR - https://linkinghub.elsevier.com/retrieve/pii/S0006-3495(22)00766-4
N2 - Intrinsically disordered proteins (IDPs) or intrinsically disordered regions (IDRs) is a class of biologically important proteins exhibiting specific biophysical characteristics. They lack a hydrophobic core, and their conformational behavior is strongly influenced by electrostatic interactions. IDPs and IDRs are highly dynamic, and a characterization of the motions of IDPs and IDRs is essential for their physically correct description. NMR together with molecular dynamics simulations are the methods best suited to such a task because they provide information about dynamics of proteins with atomistic resolution. Here, we present a study of motions of a disordered C-terminal domain of the delta subunit of RNA polymerase from Bacillus subtilis. Positively and negatively charged residues in the studied domain form transient electrostatic contacts critical for the biological function. Our study is focused on investigation of ps-ns dynamics of backbone of the delta subunit based on analysis of amide 15N NMR relaxation data and molecular dynamics simulations. In order to extend an informational content of NMR data to lower frequencies, which are more sensitive to slower motions, we combined standard (high-field) NMR relaxation experiments with high-resolution relaxometry. Altogether, we collected data reporting the relaxation at 12 different magnetic fields, resulting in an unprecedented data set. Our results document that the analysis of such data provides a consistent description of dynamics and confirms the validity of so far used protocols of the analysis of dynamics of IDPs also for a partially folded protein. In addition, the potential to access detailed description of motions at the timescale of tens of ns with the help of relaxometry data is discussed. Interestingly, in our case, it appears to be mostly relevant for a region involved in the formation of temporary contacts within the disordered region, which was previously proven to be biologically important.
ER -
SALVI, Nicola, Vojtěch ZAPLETAL, Zuzana JASEŇÁKOVÁ, Milan ZACHRDLA, Petr PADRTA, Subhash NARASIMHAN, Thorsten MARQUARDSEN, Jean-Max TYBURN, Lukáš ŽÍDEK, Martin BLACKLEDGE, Fabien FERRAGE and Pavel KADEŘÁVEK. Convergent views on disordered protein dynamics from NMR and computational approaches. \textit{BIOPHYSICAL JOURNAL}. UNITED STATES: CELL PRESS, 2022, vol.~121, No~20, p.~3785-3794. ISSN~0006-3495. Available from: https://dx.doi.org/10.1016/j.bpj.2022.09.016.
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