Nanoscale dynamics of protein assembly networks in supersaturated solutions

Matsushita, Y.; Sekiguchi, H.; Jae Wong, C.; Nishijima, M.; Ikezaki, K.; Hamada, D.; Goto, Y.; Sasaki, Y. C.

doi:https://doi.org/10.1038/s41598-017-14022-7

Nanoscale dynamics of protein assembly networks in supersaturated solutions

Matsushita, Y.; Sekiguchi, H.; Jae Wong, C. et al.

Scientific Reports, 2017, 7, 13883

Number of Access:1,081（2025-08-30 11:33 Counts）

Identifier to cite or link to this item: https://hdl.handle.net/11094/71265

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Title	Nanoscale dynamics of protein assembly networks in supersaturated solutions
Creator	CreatorName Matsushita, Y.
	NRID 1000000401563 1000000401563 CreatorName Sekiguchi, H.
	CreatorName Jae Wong, C.
	CreatorName Nishijima, M.
	CreatorName Ikezaki, K.
	CreatorName Hamada, D.
	NRID 1000040153770 1000040153770 researchmap permalink read0014440 read0014440 CreatorName Goto, Y.
	NRID 1000030344401 1000030344401 CreatorName Sasaki, Y. C.
Description	Y. Matsushita, H. Sekiguchi, C. Jae Wong, M. Nishijima, K. Ikezaki, D. Hamada, Y. Goto & Y. C. Sasaki "Nanoscale Dynamics of Protein Assembly Networks in Supersaturated Solutions", Scientific Reports, Volume 7, Article number: 13883, Springer Nature, 2017
Abstract	Proteins in solution are conventionally considered macromolecules. Dynamic microscopic structures in supersaturated protein solutions have received increasing attention in the study of protein crystallisation and the formation of misfolded aggregates. Here, we present a method for observing rotational dynamic structures that can detect the interaction of nanoscale lysozyme protein networks via diffracted X-ray tracking (DXT). Our DXT analysis demonstrated that the rearrangement behaviours of lysozyme networks or clusters, which are driven by local density and concentration fluctuations, generate force fields on the femtonewton to attonewton (fN – aN) scale. This quantitative parameter was previously observed in our experiments on supersaturated inorganic solutions. This commonality provides a way to clarify the solution structures of a variety of supersaturated solutions as well as to control nucleation and crystallisation in supersaturated solutions.
Publisher	Springer Nature
Source Title	Scientific Reports
Volume (Issue)	7
Page	13883
Date of Issued	2017-11
Language	English
Handle URL	https://hdl.handle.net/11094/71265
eISSN	20452322
Relation.isIdenticalTo	DOI (Publisher Version) https://doi.org/10.1038/s41598-017-14022-7
Access Rights	open access
CopyRight	© 2017 The Author(s). This article is licensed under a Creative Commons Attribution 4.0 International License.
oaire:version	Version of Record
Category	学術雑誌論文 Journal Article

Resource Type	journal article
Local Type	Journal Article
DCMI Type	Text
DCTERMS.bibliographicCitation	Scientific Reports. 2017, 7, p. 13883
DC.title	Nanoscale dynamics of protein assembly networks in supersaturated solutions
DC.creator	Matsushita, Y.
	Sekiguchi, H.
	Jae Wong, C.
	Nishijima, M.
	Ikezaki, K.
	Hamada, D.
	Goto, Y.
	Sasaki, Y. C.
DC.publisher	Springer Nature
DC.language' scheme='DCTERMS.RFC1766	English
DC.type' scheme='DCTERMS.DCMIType	Text
DCTERMS.issued' scheme='DCTERMS.W3CDTF	2017-11
DC.identifier	https://doi.org/10.1038/s41598-017-14022-7
DC.description	Y. Matsushita, H. Sekiguchi, C. Jae Wong, M. Nishijima, K. Ikezaki, D. Hamada, Y. Goto & Y. C. Sasaki "Nanoscale Dynamics of Protein Assembly Networks in Supersaturated Solutions", Scientific Reports, Volume 7, Article number: 13883, Springer Nature, 2017
DCTERMS.abstract	Proteins in solution are conventionally considered macromolecules. Dynamic microscopic structures in supersaturated protein solutions have received increasing attention in the study of protein crystallisation and the formation of misfolded aggregates. Here, we present a method for observing rotational dynamic structures that can detect the interaction of nanoscale lysozyme protein networks via diffracted X-ray tracking (DXT). Our DXT analysis demonstrated that the rearrangement behaviours of lysozyme networks or clusters, which are driven by local density and concentration fluctuations, generate force fields on the femtonewton to attonewton (fN – aN) scale. This quantitative parameter was previously observed in our experiments on supersaturated inorganic solutions. This commonality provides a way to clarify the solution structures of a variety of supersaturated solutions as well as to control nucleation and crystallisation in supersaturated solutions.
DC.rights	© 2017 The Author(s). This article is licensed under a Creative Commons Attribution 4.0 International License.
DC.format	71265
citation_title	Nanoscale dynamics of protein assembly networks in supersaturated solutions
citation_author	Matsushita, Y.
	Sekiguchi, H.
	Jae Wong, C.
	Nishijima, M.
	Ikezaki, K.
	Hamada, D.
	Goto, Y.
	Sasaki, Y. C.
citation_publisher	Springer Nature
citation_language	English
citation_date	2017-11
citation_journal_title	Scientific Reports
citation_volume	7
citation_firstpage	13883
citation_doi	https://doi.org/10.1038/s41598-017-14022-7
citation_public_url	https://hdl.handle.net/11094/71265

Nanoscale dynamics of protein assembly networks in supersaturated solutions

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