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1osa

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==About this Structure==
==About this Structure==
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[[1osa]] is a 1 chain structure of [[Calmodulin]] with sequence from [http://en.wikipedia.org/wiki/Paramecium_tetraurelia Paramecium tetraurelia]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OSA OCA].
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[[1osa]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Paramecium_tetraurelia Paramecium tetraurelia]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OSA OCA].
==See Also==
==See Also==

Revision as of 05:39, 20 October 2012

Template:STRUCTURE 1osa

Contents

CRYSTAL STRUCTURE OF RECOMBINANT PARAMECIUM TETRAURELIA CALMODULIN AT 1.68 ANGSTROMS RESOLUTION

Template:ABSTRACT PUBMED 15299476

About this Structure

1osa is a 1 chain structure with sequence from Paramecium tetraurelia. Full crystallographic information is available from OCA.

See Also

Reference

  • Ban C, Ramakrishnan B, Ling KY, Kung C, Sundaralingam M. Structure of the recombinant Paramecium tetraurelia calmodulin at 1.68 A resolution. Acta Crystallogr D Biol Crystallogr. 1994 Jan 1;50(Pt 1):50-63. PMID:15299476 doi:10.1107/S0907444993007991
  • Wall ME, Subramaniam S, Phillips GN Jr. Protein structure determination using a database of interatomic distance probabilities. Protein Sci. 1999 Dec;8(12):2720-7. PMID:10631988 doi:10.1110/ps.8.12.2720
  • Ermolenko DN, Thomas ST, Aurora R, Gronenborn AM, Makhatadze GI. Hydrophobic interactions at the Ccap position of the C-capping motif of alpha-helices. J Mol Biol. 2002 Sep 6;322(1):123-35. PMID:12215419
  • Biekofsky RR, Turjanski AG, Estrin DA, Feeney J, Pastore A. Ab initio study of NMR 15N chemical shift differences induced by Ca2+ binding to EF-hand proteins. Biochemistry. 2004 Jun 1;43(21):6554-64. PMID:15157088 doi:10.1021/bi0497852
  • Uchikoga N, Takahashi SY, Ke R, Sonoyama M, Mitaku S. Electric charge balance mechanism of extended soluble proteins. Protein Sci. 2005 Jan;14(1):74-80. Epub 2004 Dec 2. PMID:15576568 doi:10.1110/ps.04984505

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