Dynamics of proteins with different molecular structures under solution condition

Abstract Incoherent quasielastic neutron scattering (iQENS) is a fascinating technique for investigating the internal dynamics of protein. However, low flux of neutron beam, low signal to noise ratio of QENS spectrometers and unavailability of well-established analyzing method have been obstacles fo...

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Autores principales:	Rintaro Inoue, Takashi Oda, Hiroshi Nakagawa, Taiki Tominaga, Tomohide Saio, Yukinobu Kawakita, Masahiro Shimizu, Aya Okuda, Ken Morishima, Nobuhiro Sato, Reiko Urade, Mamoru Sato, Masaaki Sugiyama
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2020
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/802927b816be4ad28bcef6152cb0aa14
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spelling	oai:doaj.org-article:802927b816be4ad28bcef6152cb0aa142021-12-02T11:43:44ZDynamics of proteins with different molecular structures under solution condition10.1038/s41598-020-78311-42045-2322https://doaj.org/article/802927b816be4ad28bcef6152cb0aa142020-12-01T00:00:00Zhttps://doi.org/10.1038/s41598-020-78311-4https://doaj.org/toc/2045-2322Abstract Incoherent quasielastic neutron scattering (iQENS) is a fascinating technique for investigating the internal dynamics of protein. However, low flux of neutron beam, low signal to noise ratio of QENS spectrometers and unavailability of well-established analyzing method have been obstacles for studying internal dynamics under physiological condition (in solution). The recent progress of neutron source and spectrometer provide the fine iQENS profile with high statistics and as well the progress of computational technique enable us to quantitatively reveal the internal dynamic from the obtained iQENS profile. The internal dynamics of two proteins, globular domain protein (GDP) and intrinsically disordered protein (IDP) in solution, were measured with the state-of-the art QENS spectrometer and then revealed with the newly developed analyzing method. It was clarified that the average relaxation rate of IDP was larger than that of GDP and the fraction of mobile H atoms of IDP was also much higher than that of GDP. Combined with the structural analysis and the calculation of solvent accessible surface area of amino acid residue, it was concluded that the internal dynamics were related to the highly solvent exposed amino acid residues depending upon protein’s structure.Rintaro InoueTakashi OdaHiroshi NakagawaTaiki TominagaTomohide SaioYukinobu KawakitaMasahiro ShimizuAya OkudaKen MorishimaNobuhiro SatoReiko UradeMamoru SatoMasaaki SugiyamaNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 10, Iss 1, Pp 1-10 (2020)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Rintaro Inoue Takashi Oda Hiroshi Nakagawa Taiki Tominaga Tomohide Saio Yukinobu Kawakita Masahiro Shimizu Aya Okuda Ken Morishima Nobuhiro Sato Reiko Urade Mamoru Sato Masaaki Sugiyama Dynamics of proteins with different molecular structures under solution condition
description	Abstract Incoherent quasielastic neutron scattering (iQENS) is a fascinating technique for investigating the internal dynamics of protein. However, low flux of neutron beam, low signal to noise ratio of QENS spectrometers and unavailability of well-established analyzing method have been obstacles for studying internal dynamics under physiological condition (in solution). The recent progress of neutron source and spectrometer provide the fine iQENS profile with high statistics and as well the progress of computational technique enable us to quantitatively reveal the internal dynamic from the obtained iQENS profile. The internal dynamics of two proteins, globular domain protein (GDP) and intrinsically disordered protein (IDP) in solution, were measured with the state-of-the art QENS spectrometer and then revealed with the newly developed analyzing method. It was clarified that the average relaxation rate of IDP was larger than that of GDP and the fraction of mobile H atoms of IDP was also much higher than that of GDP. Combined with the structural analysis and the calculation of solvent accessible surface area of amino acid residue, it was concluded that the internal dynamics were related to the highly solvent exposed amino acid residues depending upon protein’s structure.
format	article
author	Rintaro Inoue Takashi Oda Hiroshi Nakagawa Taiki Tominaga Tomohide Saio Yukinobu Kawakita Masahiro Shimizu Aya Okuda Ken Morishima Nobuhiro Sato Reiko Urade Mamoru Sato Masaaki Sugiyama
author_facet	Rintaro Inoue Takashi Oda Hiroshi Nakagawa Taiki Tominaga Tomohide Saio Yukinobu Kawakita Masahiro Shimizu Aya Okuda Ken Morishima Nobuhiro Sato Reiko Urade Mamoru Sato Masaaki Sugiyama
author_sort	Rintaro Inoue
title	Dynamics of proteins with different molecular structures under solution condition
title_short	Dynamics of proteins with different molecular structures under solution condition
title_full	Dynamics of proteins with different molecular structures under solution condition
title_fullStr	Dynamics of proteins with different molecular structures under solution condition
title_full_unstemmed	Dynamics of proteins with different molecular structures under solution condition
title_sort	dynamics of proteins with different molecular structures under solution condition
publisher	Nature Portfolio
publishDate	2020
url	https://doaj.org/article/802927b816be4ad28bcef6152cb0aa14
work_keys_str_mv	AT rintaroinoue dynamicsofproteinswithdifferentmolecularstructuresundersolutioncondition AT takashioda dynamicsofproteinswithdifferentmolecularstructuresundersolutioncondition AT hiroshinakagawa dynamicsofproteinswithdifferentmolecularstructuresundersolutioncondition AT taikitominaga dynamicsofproteinswithdifferentmolecularstructuresundersolutioncondition AT tomohidesaio dynamicsofproteinswithdifferentmolecularstructuresundersolutioncondition AT yukinobukawakita dynamicsofproteinswithdifferentmolecularstructuresundersolutioncondition AT masahiroshimizu dynamicsofproteinswithdifferentmolecularstructuresundersolutioncondition AT ayaokuda dynamicsofproteinswithdifferentmolecularstructuresundersolutioncondition AT kenmorishima dynamicsofproteinswithdifferentmolecularstructuresundersolutioncondition AT nobuhirosato dynamicsofproteinswithdifferentmolecularstructuresundersolutioncondition AT reikourade dynamicsofproteinswithdifferentmolecularstructuresundersolutioncondition AT mamorusato dynamicsofproteinswithdifferentmolecularstructuresundersolutioncondition AT masaakisugiyama dynamicsofproteinswithdifferentmolecularstructuresundersolutioncondition
_version_	1718395352398168064

Dynamics of proteins with different molecular structures under solution condition

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