3lr2: Difference between revisions

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[[Image:3lr2.png|left|200px]]
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{{STRUCTURE_3lr2|  PDB=3lr2  |  SCENE=  }}  
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===Self-assembly of spider silk proteins is controlled by a pH-sensitive relay===
===Self-assembly of spider silk proteins is controlled by a pH-sensitive relay===
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{{ABSTRACT_PUBMED_20463740}}
{{ABSTRACT_PUBMED_20463740}}


==About this Structure==
==About this Structure==
3LR2 is a 2 chains structure with sequences from [http://en.wikipedia.org/wiki/Euprosthenops_australis Euprosthenops australis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3LR2 OCA].  
[[3lr2]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Euprosthenops_australis Euprosthenops australis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3LR2 OCA].  


==Reference==
==Reference==
<ref group="xtra">PMID:20463740</ref><references group="xtra"/>
<ref group="xtra">PMID:020463740</ref><references group="xtra"/><references/>
[[Category: Euprosthenops australis]]
[[Category: Euprosthenops australis]]
[[Category: Askarieh, G.]]
[[Category: Askarieh, G.]]
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[[Category: Self-assembly]]
[[Category: Self-assembly]]
[[Category: Structural protein]]
[[Category: Structural protein]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed May 26 08:40:42 2010''

Revision as of 02:32, 11 April 2013

Template:STRUCTURE 3lr2

Self-assembly of spider silk proteins is controlled by a pH-sensitive relaySelf-assembly of spider silk proteins is controlled by a pH-sensitive relay

Template:ABSTRACT PUBMED 20463740

About this StructureAbout this Structure

3lr2 is a 2 chain structure with sequence from Euprosthenops australis. Full crystallographic information is available from OCA.

ReferenceReference

[xtra 1]

  1. Askarieh G, Hedhammar M, Nordling K, Saenz A, Casals C, Rising A, Johansson J, Knight SD. Self-assembly of spider silk proteins is controlled by a pH-sensitive relay. Nature. 2010 May 13;465(7295):236-8. PMID:20463740 doi:10.1038/nature08962

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