1ags

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==About this Structure==
==About this Structure==
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1AGS is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AGS OCA].
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1AGS is a 2 chains structure of sequences from [http://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AGS OCA].
==Reference==
==Reference==
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A surface mutant (G82R) of a human alpha-glutathione S-transferase shows decreased thermal stability and a new mode of molecular association in the crystal., Zeng K, Rose JP, Chen HC, Strickland CL, Tu CP, Wang BC, Proteins. 1994 Nov;20(3):259-63. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/7892174 7892174]
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<ref group="xtra">PMID:7892174</ref><references group="xtra"/>
[[Category: Glutathione transferase]]
[[Category: Glutathione transferase]]
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[[Category: Single protein]]
 
[[Category: Synthetic construct]]
[[Category: Synthetic construct]]
[[Category: Rose, J P.]]
[[Category: Rose, J P.]]
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[[Category: Zeng, K.]]
[[Category: Zeng, K.]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 16:49:08 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Feb 18 00:52:14 2009''

Revision as of 22:52, 17 February 2009

Template:STRUCTURE 1ags

A SURFACE MUTANT (G82R) OF A HUMAN ALPHA-GLUTATHIONE S-TRANSFERASE SHOWS DECREASED THERMAL STABILITY AND A NEW MODE OF MOLECULAR ASSOCIATION IN THE CRYSTAL

Template:ABSTRACT PUBMED 7892174

About this Structure

1AGS is a 2 chains structure of sequences from Synthetic construct. Full crystallographic information is available from OCA.

Reference

  • Zeng K, Rose JP, Chen HC, Strickland CL, Tu CP, Wang BC. A surface mutant (G82R) of a human alpha-glutathione S-transferase shows decreased thermal stability and a new mode of molecular association in the crystal. Proteins. 1994 Nov;20(3):259-63. PMID:7892174 doi:http://dx.doi.org/10.1002/prot.340200306

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