2klf: Difference between revisions

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[[Image:2klf.png|left|200px]]
[[Image:2klf.png|left|200px]]


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==About this Structure==
==About this Structure==
2KLF is a 1 chain structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli_k-12 Escherichia coli k-12]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2KLF OCA].  
[[2klf]] is a 1 chain structure of [[Maltose-binding protein]] 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=2KLF OCA].  
 
==See Also==
*[[Maltose-binding protein|Maltose-binding protein]]


==Reference==
==Reference==
<ref group="xtra">PMID:19774576</ref><references group="xtra"/>
<ref group="xtra">PMID:019774576</ref><references group="xtra"/>
[[Category: Escherichia coli k-12]]
[[Category: Escherichia coli]]
[[Category: Bermel, W.]]
[[Category: Bermel, W.]]
[[Category: Madl, T.]]
[[Category: Madl, T.]]
[[Category: Zangger, K.]]
[[Category: Zangger, K.]]
[[Category: Maltose-binding protein]]
[[Category: Maltose-binding protein]]
[[Category: Nmr]]
[[Category: Paramagnetic relaxation]]
[[Category: Paramagnetic relaxation]]
[[Category: Periplasm]]
[[Category: Sugar transport]]
[[Category: Sugar transport]]
[[Category: Transport]]
[[Category: Transport]]
[[Category: Transport protein]]
[[Category: Transport protein]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Oct 21 09:41:22 2009''

Revision as of 18:44, 25 July 2012

File:2klf.png

Template:STRUCTURE 2klf

PERE NMR structure of maltodextrin-binding proteinPERE NMR structure of maltodextrin-binding protein

About this StructureAbout this Structure

2klf is a 1 chain structure of Maltose-binding protein with sequence from Escherichia coli. Full experimental information is available from OCA.

See AlsoSee Also

ReferenceReference

[xtra 1]

  1. Madl T, Bermel W, Zangger K. Use of relaxation enhancements in a paramagnetic environment for the structure determination of proteins using NMR spectroscopy. Angew Chem Int Ed Engl. 2009;48(44):8259-62. PMID:19774576 doi:10.1002/anie.200902561

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