256b: Difference between revisions
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Revision as of 14:32, 26 July 2012
IMPROVEMENT OF THE 2.5 ANGSTROMS RESOLUTION MODEL OF CYTOCHROME B562 BY REDETERMINING THE PRIMARY STRUCTURE AND USING MOLECULAR GRAPHICSIMPROVEMENT OF THE 2.5 ANGSTROMS RESOLUTION MODEL OF CYTOCHROME B562 BY REDETERMINING THE PRIMARY STRUCTURE AND USING MOLECULAR GRAPHICS
About this StructureAbout this Structure
256b is a 2 chain structure of Cytochrome b5 with sequence from Escherichia coli. This structure supersedes the now removed PDB entry 156b. Full crystallographic information is available from OCA.
See AlsoSee Also
ReferenceReference
[xtra 1][xtra 2][xtra 3][xtra 4][xtra 5]
- ↑ Lederer F, Glatigny A, Bethge PH, Bellamy HD, Matthew FS. Improvement of the 2.5 A resolution model of cytochrome b562 by redetermining the primary structure and using molecular graphics. J Mol Biol. 1981 Jun 5;148(4):427-48. PMID:7031264
- ↑ . PMID:007723042
- ↑ Chou KC. Does the folding type of a protein depend on its amino acid composition? FEBS Lett. 1995 Apr 17;363(1-2):127-31. PMID:7729532
- ↑ Parker MH, Hefford MA. A consensus residue analysis of loop and helix-capping residues in four-alpha-helical-bundle proteins. Protein Eng. 1997 May;10(5):487-96. PMID:9215566
- ↑ Greene LH, Higman VA. Uncovering network systems within protein structures. J Mol Biol. 2003 Dec 5;334(4):781-91. PMID:14636602