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1hdn

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Revision as of 15:35, 21 November 2012

Template:STRUCTURE 1hdn

THE HIGH-RESOLUTION STRUCTURE OF THE HISTIDINE-CONTAINING PHOSPHOCARRIER PROTEIN HPR FROM ESCHERICHIA COLI DETERMINED BY RESTRAINED MOLECULAR DYNAMICS FROM NMR NUCLEAR OVERHAUSER EFFECT DATA

Template:ABSTRACT PUBMED 8158637

About this Structure

1hdn is a 1 chain structure with sequence from Escherichia coli. Full experimental information is available from OCA.

Reference

  • van Nuland NA, Hangyi IW, van Schaik RC, Berendsen HJ, van Gunsteren WF, Scheek RM, Robillard GT. The high-resolution structure of the histidine-containing phosphocarrier protein HPr from Escherichia coli determined by restrained molecular dynamics from nuclear magnetic resonance nuclear Overhauser effect data. J Mol Biol. 1994 Apr 15;237(5):544-59. PMID:8158637 doi:http://dx.doi.org/10.1006/jmbi.1994.1254
  • 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
  • Huang JT, Tian J. Amino acid sequence predicts folding rate for middle-size two-state proteins. Proteins. 2006 May 15;63(3):551-4. PMID:16477599 doi:10.1002/prot.20911
  • Zhang J, Liu JS. On side-chain conformational entropy of proteins. PLoS Comput Biol. 2006 Dec 8;2(12):e168. PMID:17154716 doi:10.1371/journal.pcbi.0020168

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