3agh: Difference between revisions
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[[Image:3agh.jpg|left|200px]] | |||
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{{STRUCTURE_3agh| PDB=3agh | SCENE= }} | |||
===X-ray analysis of lysozyme in the presence of 200 mM Arg=== | |||
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{{ABSTRACT_PUBMED_21084280}} | |||
==About this Structure== | |||
[[3agh]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3AGH OCA]. | |||
==Reference== | |||
<ref group="xtra">PMID:21084280</ref><references group="xtra"/> | |||
[[Category: Gallus gallus]] | |||
[[Category: Lysozyme]] | |||
[[Category: Baba, S.]] | |||
[[Category: Hasegawa, K.]] | |||
[[Category: Ito, L.]] | |||
[[Category: Kumasaka, T.]] | |||
[[Category: Shiraki, K.]] | |||
Revision as of 10:08, 23 March 2011
X-ray analysis of lysozyme in the presence of 200 mM ArgX-ray analysis of lysozyme in the presence of 200 mM Arg
Template:ABSTRACT PUBMED 21084280
About this StructureAbout this Structure
3agh is a 1 chain structure with sequence from Gallus gallus. Full crystallographic information is available from OCA.
ReferenceReference
- ↑ Ito L, Shiraki K, Matsuura T, Okumura M, Hasegawa K, Baba S, Yamaguchi H, Kumasaka T. High-resolution X-ray analysis reveals binding of arginine to aromatic residues of lysozyme surface: implication of suppression of protein aggregation by arginine. Protein Eng Des Sel. 2011 Mar;24(3):269-74. Epub 2010 Nov 17. PMID:21084280 doi:10.1093/protein/gzq101