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3agh
From Proteopedia
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| - | [[Image:3agh. | + | [[Image:3agh.png|left|200px]] |
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{{STRUCTURE_3agh| PDB=3agh | SCENE= }} | {{STRUCTURE_3agh| PDB=3agh | SCENE= }} | ||
===X-ray analysis of lysozyme in the presence of 200 mM Arg=== | ===X-ray analysis of lysozyme in the presence of 200 mM Arg=== | ||
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{{ABSTRACT_PUBMED_21084280}} | {{ABSTRACT_PUBMED_21084280}} | ||
==About this Structure== | ==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]. | + | [[3agh]] is a 1 chain structure of [[Hen Egg-White (HEW) Lysozyme]] 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]. |
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| + | ==See Also== | ||
| + | *[[Hen Egg-White (HEW) Lysozyme|Hen Egg-White (HEW) Lysozyme]] | ||
==Reference== | ==Reference== | ||
| - | <ref group="xtra">PMID: | + | <ref group="xtra">PMID:021084280</ref><references group="xtra"/> |
[[Category: Gallus gallus]] | [[Category: Gallus gallus]] | ||
[[Category: Lysozyme]] | [[Category: Lysozyme]] | ||
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[[Category: Kumasaka, T.]] | [[Category: Kumasaka, T.]] | ||
[[Category: Shiraki, K.]] | [[Category: Shiraki, K.]] | ||
| + | [[Category: Allergen]] | ||
| + | [[Category: Antimicrobial]] | ||
| + | [[Category: Arginine]] | ||
| + | [[Category: Bacteriolytic enzyme]] | ||
| + | [[Category: Disulfide bond]] | ||
| + | [[Category: Glycosidase]] | ||
| + | [[Category: Hydrolase]] | ||
| + | [[Category: Lysozyme]] | ||
Revision as of 23:10, 26 July 2012
Contents |
X-ray analysis of lysozyme in the presence of 200 mM Arg
Template:ABSTRACT PUBMED 21084280
About this Structure
3agh is a 1 chain structure of Hen Egg-White (HEW) Lysozyme with sequence from Gallus gallus. Full crystallographic information is available from OCA.
See Also
Reference
- 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
Categories: Gallus gallus | Lysozyme | Baba, S. | Hasegawa, K. | Ito, L. | Kumasaka, T. | Shiraki, K. | Allergen | Antimicrobial | Arginine | Bacteriolytic enzyme | Disulfide bond | Glycosidase | Hydrolase
