2btg
From Proteopedia
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[[Image:2btg.png|left|200px]] | [[Image:2btg.png|left|200px]] | ||
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===PERIPHERAL-SUBUNIT BINDING DOMAINS FROM MESOPHILIC, THERMOPHILIC, AND HYPERTHERMOPHILIC BACTERIA FOLD BY ULTRAFAST, APPARENTLY TWO-STATE TRANSITIONS=== | ===PERIPHERAL-SUBUNIT BINDING DOMAINS FROM MESOPHILIC, THERMOPHILIC, AND HYPERTHERMOPHILIC BACTERIA FOLD BY ULTRAFAST, APPARENTLY TWO-STATE TRANSITIONS=== | ||
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{{ABSTRACT_PUBMED_16168437}} | {{ABSTRACT_PUBMED_16168437}} | ||
==About this Structure== | ==About this Structure== | ||
- | + | [[2btg]] is a 1 chain structure of [[2-Oxoglutarate Dehydrogenase]] with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BTG OCA]. | |
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+ | ==See Also== | ||
+ | *[[2-Oxoglutarate Dehydrogenase|2-Oxoglutarate Dehydrogenase]] | ||
==Reference== | ==Reference== | ||
- | <ref group="xtra">PMID: | + | <ref group="xtra">PMID:016168437</ref><references group="xtra"/> |
[[Category: Dihydrolipoyllysine-residue succinyltransferase]] | [[Category: Dihydrolipoyllysine-residue succinyltransferase]] | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
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[[Category: Lipoyl]] | [[Category: Lipoyl]] | ||
[[Category: Transferase]] | [[Category: Transferase]] | ||
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- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 22 10:30:09 2009'' |
Revision as of 10:03, 27 July 2012
Contents |
PERIPHERAL-SUBUNIT BINDING DOMAINS FROM MESOPHILIC, THERMOPHILIC, AND HYPERTHERMOPHILIC BACTERIA FOLD BY ULTRAFAST, APPARENTLY TWO-STATE TRANSITIONS
Template:ABSTRACT PUBMED 16168437
About this Structure
2btg is a 1 chain structure of 2-Oxoglutarate Dehydrogenase with sequence from Escherichia coli. Full experimental information is available from OCA.
See Also
Reference
- Ferguson N, Sharpe TD, Schartau PJ, Sato S, Allen MD, Johnson CM, Rutherford TJ, Fersht AR. Ultra-fast barrier-limited folding in the peripheral subunit-binding domain family. J Mol Biol. 2005 Oct 21;353(2):427-46. PMID:16168437 doi:10.1016/j.jmb.2005.08.031