256b: Difference between revisions
From Proteopedia
Jump to navigationJump to search
No edit summary |
m Protected "256b" [edit=sysop:move=sysop] |
(No difference)
| |
Revision as of 11:32, 26 July 2012
IMPROVEMENT OF THE 2.5 ANGSTROMS RESOLUTION MODEL OF CYTOCHROME B562 BY REDETERMINING THE PRIMARY STRUCTURE AND USING MOLECULAR GRAPHICS
About 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 Also
Reference
- 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
- Hamada K, Bethge PH, Mathews FS. Refined structure of cytochrome b562 from Escherichia coli at 1.4 A resolution. J Mol Biol. 1995 Apr 14;247(5):947-62. doi: 10.1006/jmbi.1995.0192. PMID:7723042 doi:https://dx.doi.org/10.1006/jmbi.1995.0192
- 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
