Quantitative comparison of protein dynamics in live cells and in vitro by in-cell 19F-NMRElectronic supplementary information (ESI) available. See DOI: 10.1039/c3cc39205h
Here we describe how a 19 F-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...
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| creator | Takaoka, Yousuke Kioi, Yoshiyuki Morito, Akira Otani, Junji Arita, Kyohei Ashihara, Eishi Ariyoshi, Mariko Tochio, Hidehito Shirakawa, Masahiro Hamachi, Itaru |
| description | Here we describe how a
19
F-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.
The unprecedented quantitative comparison of the protein's dynamics in live cells and
in vitro
is presented. |
| doi_str_mv | 10.1039/c3cc39205h |
| format | Article |
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19
F-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.
The unprecedented quantitative comparison of the protein's dynamics in live cells and
in vitro
is presented.</description><identifier>ISSN: 1359-7345</identifier><identifier>EISSN: 1364-548X</identifier><identifier>DOI: 10.1039/c3cc39205h</identifier><language>eng</language><creationdate>2013-03</creationdate><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>315,781,785,27929,27930</link.rule.ids></links><search><creatorcontrib>Takaoka, Yousuke</creatorcontrib><creatorcontrib>Kioi, Yoshiyuki</creatorcontrib><creatorcontrib>Morito, Akira</creatorcontrib><creatorcontrib>Otani, Junji</creatorcontrib><creatorcontrib>Arita, Kyohei</creatorcontrib><creatorcontrib>Ashihara, Eishi</creatorcontrib><creatorcontrib>Ariyoshi, Mariko</creatorcontrib><creatorcontrib>Tochio, Hidehito</creatorcontrib><creatorcontrib>Shirakawa, Masahiro</creatorcontrib><creatorcontrib>Hamachi, Itaru</creatorcontrib><title>Quantitative comparison of protein dynamics in live cells and in vitro by in-cell 19F-NMRElectronic supplementary information (ESI) available. See DOI: 10.1039/c3cc39205h</title><description>Here we describe how a
19
F-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.
The unprecedented quantitative comparison of the protein's dynamics in live cells and
in vitro
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19
F-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.
The unprecedented quantitative comparison of the protein's dynamics in live cells and
in vitro
is presented.</abstract><doi>10.1039/c3cc39205h</doi><tpages>3</tpages></addata></record> |
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| source | Royal Society Of Chemistry Journals 2008-; Alma/SFX Local Collection |
| title | Quantitative comparison of protein dynamics in live cells and in vitro by in-cell 19F-NMRElectronic supplementary information (ESI) available. See DOI: 10.1039/c3cc39205h |
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