153l
From Proteopedia
(Difference between revisions)
Line 1: | Line 1: | ||
- | {{Seed}} | ||
[[Image:153l.png|left|200px]] | [[Image:153l.png|left|200px]] | ||
Line 20: | Line 19: | ||
==About this Structure== | ==About this Structure== | ||
- | + | [[153l]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Anser_anser_anser Anser anser anser]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=153L OCA]. | |
+ | |||
+ | ==See Also== | ||
+ | *[[Hen Egg-White (HEW) Lysozyme]] | ||
==Reference== | ==Reference== | ||
- | <ref group="xtra">PMID: | + | <ref group="xtra">PMID:007823320</ref><ref group="xtra">PMID:011917145</ref><ref group="xtra">PMID:014695246</ref><references group="xtra"/> |
[[Category: Anser anser anser]] | [[Category: Anser anser anser]] | ||
[[Category: Lysozyme]] | [[Category: Lysozyme]] | ||
Line 29: | Line 31: | ||
[[Category: Matthews, B W.]] | [[Category: Matthews, B W.]] | ||
[[Category: Weaver, L H.]] | [[Category: Weaver, L H.]] | ||
- | |||
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Sep 21 19:32:12 2009'' |
Revision as of 11:55, 27 April 2011
Contents |
THE REFINED STRUCTURES OF GOOSE LYSOZYME AND ITS COMPLEX WITH A BOUND TRISACCHARIDE SHOW THAT THE "GOOSE-TYPE LYSOZYMES LACK A CATALYTIC ASPARTATE
Template:ABSTRACT PUBMED 7823320
About this Structure
153l is a 1 chain structure with sequence from Anser anser anser. Full crystallographic information is available from OCA.
See Also
Reference
- Weaver LH, Grutter MG, Matthews BW. The refined structures of goose lysozyme and its complex with a bound trisaccharide show that the "goose-type" lysozymes lack a catalytic aspartate residue. J Mol Biol. 1995 Jan 6;245(1):54-68. PMID:7823320
- Bhattacharyya R, Samanta U, Chakrabarti P. Aromatic-aromatic interactions in and around alpha-helices. Protein Eng. 2002 Feb;15(2):91-100. PMID:11917145
- Sandelin E. On hydrophobicity and conformational specificity in proteins. Biophys J. 2004 Jan;86(1 Pt 1):23-30. PMID:14695246 doi:10.1016/S0006-3495(04)74080-1