451c: Difference between revisions

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{{Seed}}
[[Image:451c.png|left|200px]]
[[Image:451c.png|left|200px]]


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==About this Structure==
==About this Structure==
451C is a 1 chain structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=451C OCA].  
[[451c]] is a 1 chain structure of [[Cytochrome c]] with sequence from [http://en.wikipedia.org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=451C OCA].  
 
==See Also==
*[[Cytochrome c|Cytochrome c]]


==Reference==
==Reference==
<ref group="xtra">PMID:6283101</ref><references group="xtra"/>
<ref group="xtra">PMID:006283101</ref><ref group="xtra">PMID:009078240</ref><ref group="xtra">PMID:011604529</ref><ref group="xtra">PMID:011734033</ref><ref group="xtra">PMID:011917145</ref><ref group="xtra">PMID:015267926</ref><ref group="xtra">PMID:017154716</ref><references group="xtra"/>
[[Category: Pseudomonas aeruginosa]]
[[Category: Pseudomonas aeruginosa]]
[[Category: Dickerson, R E.]]
[[Category: Dickerson, R E.]]
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[[Category: Takano, T.]]
[[Category: Takano, T.]]
[[Category: Electron transport]]
[[Category: Electron transport]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 15:15:38 2009''

Revision as of 21:06, 26 July 2012

File:451c.png

Template:STRUCTURE 451c

STRUCTURE OF CYTOCHROME C551 FROM P. AERUGINOSA REFINED AT 1.6 ANGSTROMS RESOLUTION AND COMPARISON OF THE TWO REDOX FORMS

About this Structure

451c is a 1 chain structure of Cytochrome c with sequence from Pseudomonas aeruginosa. Full crystallographic information is available from OCA.

See Also

Reference

  1. Matsuura Y, Takano T, Dickerson RE. Structure of cytochrome c551 from Pseudomonas aeruginosa refined at 1.6 A resolution and comparison of the two redox forms. J Mol Biol. 1982 Apr 5;156(2):389-409. PMID:6283101
  2. Cutruzzola F, Ciabatti I, Rolli G, Falcinelli S, Arese M, Ranghino G, Anselmino A, Zennaro E, Silvestrini MC. Expression and characterization of Pseudomonas aeruginosa cytochrome c-551 and two site-directed mutants: role of tryptophan 56 in the modulation of redox properties. Biochem J. 1997 Feb 15;322 ( Pt 1)(Pt 1):35-42. doi: 10.1042/bj3220035. PMID:9078240 doi:https://dx.doi.org/10.1042/bj3220035
  3. Hayward S. Peptide-plane flipping in proteins. Protein Sci. 2001 Nov;10(11):2219-27. PMID:11604529 doi:10.1110/ps.23101
  4. 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
  5. Bhattacharyya R, Samanta U, Chakrabarti P. Aromatic-aromatic interactions in and around alpha-helices. Protein Eng. 2002 Feb;15(2):91-100. PMID:11917145
  6. Feig M, Im W, Brooks CL 3rd. Implicit solvation based on generalized Born theory in different dielectric environments. J Chem Phys. 2004 Jan 8;120(2):903-11. PMID:15267926 doi:10.1063/1.1631258
  7. 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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