1hdn
From Proteopedia
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===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=== | ===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=== | ||
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{{ABSTRACT_PUBMED_8158637}} | {{ABSTRACT_PUBMED_8158637}} | ||
==About this Structure== | ==About this Structure== | ||
| - | + | [[1hdn]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HDN OCA]. | |
==Reference== | ==Reference== | ||
| - | <ref group="xtra">PMID: | + | <ref group="xtra">PMID:008158637</ref><ref group="xtra">PMID:011734033</ref><ref group="xtra">PMID:016477599</ref><ref group="xtra">PMID:017154716</ref><references group="xtra"/> |
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Nuland, N A.J Van.]] | [[Category: Nuland, N A.J Van.]] | ||
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[[Category: Scheek, R M.]] | [[Category: Scheek, R M.]] | ||
[[Category: Phosphotransferase]] | [[Category: Phosphotransferase]] | ||
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| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Feb 18 00:26:32 2009'' | ||
Revision as of 15:35, 21 November 2012
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
