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1hst
From Proteopedia
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===CRYSTAL STRUCTURE OF GLOBULAR DOMAIN OF HISTONE H5 AND ITS IMPLICATIONS FOR NUCLEOSOME BINDING=== | ===CRYSTAL STRUCTURE OF GLOBULAR DOMAIN OF HISTONE H5 AND ITS IMPLICATIONS FOR NUCLEOSOME BINDING=== | ||
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==About this Structure== | ==About this Structure== | ||
| - | + | [[1hst]] is a 2 chain structure of [[Histone]] 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=1HST OCA]. | |
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| + | ==See Also== | ||
| + | *[[Histone|Histone]] | ||
==Reference== | ==Reference== | ||
| - | <ref group="xtra">PMID: | + | <ref group="xtra">PMID:008384699</ref><ref group="xtra">PMID:011734033</ref><ref group="xtra">PMID:014695246</ref><references group="xtra"/> |
[[Category: Gallus gallus]] | [[Category: Gallus gallus]] | ||
[[Category: Finch, J T.]] | [[Category: Finch, J T.]] | ||
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[[Category: Sweet, R M.]] | [[Category: Sweet, R M.]] | ||
[[Category: Chromosomal protein]] | [[Category: Chromosomal protein]] | ||
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Revision as of 15:36, 27 July 2012
Contents |
CRYSTAL STRUCTURE OF GLOBULAR DOMAIN OF HISTONE H5 AND ITS IMPLICATIONS FOR NUCLEOSOME BINDING
Template:ABSTRACT PUBMED 8384699
About this Structure
1hst is a 2 chain structure of Histone with sequence from Gallus gallus. Full crystallographic information is available from OCA.
See Also
Reference
- Ramakrishnan V, Finch JT, Graziano V, Lee PL, Sweet RM. Crystal structure of globular domain of histone H5 and its implications for nucleosome binding. Nature. 1993 Mar 18;362(6417):219-23. PMID:8384699 doi:http://dx.doi.org/10.1038/362219a0
- Sharman GJ, Griffiths-Jones SR, Jourdan M, Searle MS. Effects of amino acid phi,psi propensities and secondary structure interactions in modulating H alpha chemical shifts in peptide and protein beta-sheet. J Am Chem Soc. 2001 Dec 12;123(49):12318-24. PMID:11734033
- 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
