1hfy
From Proteopedia
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{{STRUCTURE_1hfy| PDB=1hfy | SCENE= }} | {{STRUCTURE_1hfy| PDB=1hfy | SCENE= }} | ||
===ALPHA-LACTALBUMIN=== | ===ALPHA-LACTALBUMIN=== | ||
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==About this Structure== | ==About this Structure== | ||
| - | + | [[1hfy]] is a 2 chain structure of [[Lactalbumin]] with sequence from [http://en.wikipedia.org/wiki/Capra_hircus Capra hircus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HFY OCA]. | |
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| + | ==See Also== | ||
| + | *[[Lactalbumin|Lactalbumin]] | ||
==Reference== | ==Reference== | ||
| - | <ref group="xtra">PMID: | + | <ref group="xtra">PMID:008805552</ref><ref group="xtra">PMID:011112553</ref><ref group="xtra">PMID:020080106</ref><references group="xtra"/> |
[[Category: Capra hircus]] | [[Category: Capra hircus]] | ||
[[Category: Lactose synthase]] | [[Category: Lactose synthase]] | ||
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[[Category: Lactose]] | [[Category: Lactose]] | ||
[[Category: Lactose synthase component]] | [[Category: Lactose synthase component]] | ||
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Revision as of 04:02, 27 July 2012
Contents |
ALPHA-LACTALBUMIN
Template:ABSTRACT PUBMED 8805552
About this Structure
1hfy is a 2 chain structure of Lactalbumin with sequence from Capra hircus. Full crystallographic information is available from OCA.
See Also
Reference
- Pike AC, Brew K, Acharya KR. Crystal structures of guinea-pig, goat and bovine alpha-lactalbumin highlight the enhanced conformational flexibility of regions that are significant for its action in lactose synthase. Structure. 1996 Jun 15;4(6):691-703. PMID:8805552
- Chaudhuri TK, Arai M, Terada TP, Ikura T, Kuwajima K. Equilibrium and kinetic studies on folding of the authentic and recombinant forms of human alpha-lactalbumin by circular dichroism spectroscopy. Biochemistry. 2000 Dec 19;39(50):15643-51. PMID:11112553
- Nakamura T, Makabe K, Tomoyori K, Maki K, Mukaiyama A, Kuwajima K. Different folding pathways taken by highly homologous proteins, goat alpha-lactalbumin and canine milk lysozyme. J Mol Biol. 2010 Mar 12;396(5):1361-78. Epub 2010 Jan 18. PMID:20080106 doi:10.1016/j.jmb.2010.01.021
