1cyu: Difference between revisions

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==About this Structure==
==About this Structure==
1CYU is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CYU OCA].  
1CYU is a 1 chain structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CYU OCA].  


==Reference==
==Reference==
Solution structure of a human cystatin A variant, cystatin A2-98 M65L, by NMR spectroscopy. A possible role of the interactions between the N- and C-termini to maintain the inhibitory active form of cystatin A., Tate S, Ushioda T, Utsunomiya-Tate N, Shibuya K, Ohyama Y, Nakano Y, Kaji H, Inagaki F, Samejima T, Kainosho M, Biochemistry. 1995 Nov 14;34(45):14637-48. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/7578072 7578072]
<ref group="xtra">PMID:7578072</ref><references group="xtra"/>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Kainosho, M.]]
[[Category: Kainosho, M.]]
[[Category: Samejima, T.]]
[[Category: Samejima, T.]]
Line 32: Line 31:
[[Category: Ushioda, T.]]
[[Category: Ushioda, T.]]


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Revision as of 19:27, 17 February 2009

File:1cyu.png

Template:STRUCTURE 1cyu

SOLUTION NMR STRUCTURE OF RECOMBINANT HUMAN CYSTATIN A UNDER THE CONDITION OF PH 3.8 AND 310KSOLUTION NMR STRUCTURE OF RECOMBINANT HUMAN CYSTATIN A UNDER THE CONDITION OF PH 3.8 AND 310K

Template:ABSTRACT PUBMED 7578072

About this StructureAbout this Structure

1CYU is a 1 chain structure of sequence from Homo sapiens. Full experimental information is available from OCA.

ReferenceReference

[xtra 1]

  1. Tate S, Ushioda T, Utsunomiya-Tate N, Shibuya K, Ohyama Y, Nakano Y, Kaji H, Inagaki F, Samejima T, Kainosho M. Solution structure of a human cystatin A variant, cystatin A2-98 M65L, by NMR spectroscopy. A possible role of the interactions between the N- and C-termini to maintain the inhibitory active form of cystatin A. Biochemistry. 1995 Nov 14;34(45):14637-48. PMID:7578072

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