1lc1: Difference between revisions

Revision as of 12:18, 2 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1lc1.png

Template:STRUCTURE 1lc1

Solution Structure Of Reduced Horse Heart Cytochrome c in 30% Acetonitrile Solution, NMR Minimized Average StructureSolution Structure Of Reduced Horse Heart Cytochrome c in 30% Acetonitrile Solution, NMR Minimized Average Structure

Template:ABSTRACT PUBMED 12764601

About this StructureAbout this Structure

1LC1 is a Single protein structure of sequence from Equus caballus. Full experimental information is available from OCA.

ReferenceReference

Structure-function relationship of reduced cytochrome c probed by complete solution structure determination in 30% acetonitrile/water solution., Sivakolundu SG, Mabrouk PA, J Biol Inorg Chem. 2003 May;8(5):527-39. Epub 2003 Feb 15. PMID:12764601

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-'''Solution Structure Of Reduced Horse Heart Cytochrome c in 30% Acetonitrile Solution, NMR Minimized Average Structure'''
+===Solution Structure Of Reduced Horse Heart Cytochrome c in 30% Acetonitrile Solution, NMR Minimized Average Structure===
-==Overview==
+<!--
-The complete solution structure of ferrocytochrome c in 30% acetonitrile/70% water has been determined using high-field 1D and 2D (1)H NMR methods and deposited in the Protein Data Bank with codes 1LC1 and 1LC2. This is the first time a complete solution protein structure has been determined for a protein in nonaqueous media. Ferrocyt c retains a native protein secondary structure (five alpha-helices and two omega loops) in 30% acetonitrile. H18 and M80 residues are the axial heme ligands, as in aqueous solution. Residues believed to be axial heme ligands in the alkaline-like conformers of ferricyt c, specifically H33 and K72, are positioned close to the heme iron. The orientations of both heme propionates are markedly different in 30% acetonitrile/70% water. Comparative structural analysis of reduced cyt c in 30% acetonitrile/70% water solution with cyt c in different environments has given new insight into the cyt c folding mechanism, the electron transfer pathway, and cell apoptosis.
+The line below this paragraph, {{ABSTRACT_PUBMED_12764601}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 12764601 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_12764601}}
 ==About this Structure==
-LC1 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Equus_caballus Equus caballus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LC1 OCA].
+LC1 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Equus_caballus Equus caballus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LC1 OCA].
 ==Reference==
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 [[Category: Cytochrome c]]
 [[Category: Organic solvent]]
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