Quantitative comparison of protein dynamics in live cells and in vitro by in-cell19F-NMR

Yousuke Takaoka; Yoshiyuki Kioi; Akira Morito; Junji Otani; Kyohei Arita; Eishi Ashihara; Mariko Ariyoshi; Hidehito Tochio; Masahiro Shirakawa; Itaru Hamachi

doi:10.1039/c3cc39205h

Quantitative comparison of protein dynamics in live cells and in vitro by in-cell¹⁹F-NMR

Yousuke Takaoka, Yoshiyuki Kioi, Akira Morito, Junji Otani, Kyohei Arita, Eishi Ashihara, Mariko Ariyoshi, Hidehito Tochio, Masahiro Shirakawa, Itaru Hamachi

Research output: Contribution to journal › Article › peer-review

30 Citations (Scopus)

Abstract

Here we describe how a¹⁹F-probe incorporated into an endogenous protein by a chemical biology method revealed protein dynamics. By explicit determination of ligand-bound and unbound structures with X-ray crystallography, the quantitative comparison of the protein's dynamics in live cells and in vitro is presented. These results clearly demonstrated the greater conformational fluctuations of the intracellular protein, partially due to macromolecular crowding effects.

Original language	English
Pages (from-to)	2801-2803
Number of pages	3
Journal	Chemical Communications
Volume	49
Issue number	27
DOIs	https://doi.org/10.1039/c3cc39205h
Publication status	Published - 2013 Mar 7
Externally published	Yes

ASJC Scopus subject areas

Catalysis
Electronic, Optical and Magnetic Materials
Ceramics and Composites
Chemistry(all)
Surfaces, Coatings and Films
Metals and Alloys
Materials Chemistry

Access to Document

10.1039/c3cc39205h

Fingerprint Dive into the research topics of 'Quantitative comparison of protein dynamics in live cells and in vitro by in-cell<sup>19</sup>F-NMR'. Together they form a unique fingerprint.

Cite this

Quantitative comparison of protein dynamics in live cells and in vitro by in-cell¹⁹F-NMR. / Takaoka, Yousuke; Kioi, Yoshiyuki; Morito, Akira; Otani, Junji; Arita, Kyohei; Ashihara, Eishi; Ariyoshi, Mariko; Tochio, Hidehito; Shirakawa, Masahiro; Hamachi, Itaru.

In: Chemical Communications, Vol. 49, No. 27, 07.03.2013, p. 2801-2803.

Research output: Contribution to journal › Article › peer-review

@article{dae4b93ee55f498e9c68d70a262ebd18,

title = "Quantitative comparison of protein dynamics in live cells and in vitro by in-cell19F-NMR",

abstract = "Here we describe how a19F-probe incorporated into an endogenous protein by a chemical biology method revealed protein dynamics. By explicit determination of ligand-bound and unbound structures with X-ray crystallography, the quantitative comparison of the protein's dynamics in live cells and in vitro is presented. These results clearly demonstrated the greater conformational fluctuations of the intracellular protein, partially due to macromolecular crowding effects.",

author = "Yousuke Takaoka and Yoshiyuki Kioi and Akira Morito and Junji Otani and Kyohei Arita and Eishi Ashihara and Mariko Ariyoshi and Hidehito Tochio and Masahiro Shirakawa and Itaru Hamachi",

year = "2013",

month = mar,

day = "7",

doi = "10.1039/c3cc39205h",

language = "English",

volume = "49",

pages = "2801--2803",

journal = "Chemical Communications",

issn = "1359-7345",

publisher = "Royal Society of Chemistry",

number = "27",

}

TY - JOUR

T1 - Quantitative comparison of protein dynamics in live cells and in vitro by in-cell19F-NMR

AU - Takaoka, Yousuke

AU - Kioi, Yoshiyuki

AU - Morito, Akira

AU - Otani, Junji

AU - Arita, Kyohei

AU - Ashihara, Eishi

AU - Ariyoshi, Mariko

AU - Tochio, Hidehito

AU - Shirakawa, Masahiro

AU - Hamachi, Itaru

PY - 2013/3/7

Y1 - 2013/3/7

N2 - Here we describe how a19F-probe incorporated into an endogenous protein by a chemical biology method revealed protein dynamics. By explicit determination of ligand-bound and unbound structures with X-ray crystallography, the quantitative comparison of the protein's dynamics in live cells and in vitro is presented. These results clearly demonstrated the greater conformational fluctuations of the intracellular protein, partially due to macromolecular crowding effects.

AB - Here we describe how a19F-probe incorporated into an endogenous protein by a chemical biology method revealed protein dynamics. By explicit determination of ligand-bound and unbound structures with X-ray crystallography, the quantitative comparison of the protein's dynamics in live cells and in vitro is presented. These results clearly demonstrated the greater conformational fluctuations of the intracellular protein, partially due to macromolecular crowding effects.

UR - http://www.scopus.com/inward/record.url?scp=84874912487&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=84874912487&partnerID=8YFLogxK

U2 - 10.1039/c3cc39205h

DO - 10.1039/c3cc39205h

M3 - Article

C2 - 23440262

AN - SCOPUS:84874912487

VL - 49

SP - 2801

EP - 2803

JO - Chemical Communications

JF - Chemical Communications

SN - 1359-7345

IS - 27

ER -