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New page: left|200px<br /><applet load="1lc2" size="450" color="white" frame="true" align="right" spinBox="true" caption="1lc2" /> '''Solution Structure Of Reduced Horse Heart Cy...
 
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'''Solution Structure Of Reduced Horse Heart Cytochrome c in 30% Acetonitrile Solution, NMR 30 Structures'''<br />
'''Solution Structure Of Reduced Horse Heart Cytochrome c in 30% Acetonitrile Solution, NMR 30 Structures'''<br />


==Overview==
==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 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.


==About this Structure==
==About this Structure==
1LC2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Equus_caballus Equus caballus] with HEC as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1LC2 OCA].  
1LC2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Equus_caballus Equus caballus] with <scene name='pdbligand=HEC:'>HEC</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LC2 OCA].  


==Reference==
==Reference==
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[[Category: Equus caballus]]
[[Category: Equus caballus]]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Mabrouk, P.A.]]
[[Category: Mabrouk, P A.]]
[[Category: Sivakolundu, S.G.]]
[[Category: Sivakolundu, S G.]]
[[Category: HEC]]
[[Category: HEC]]
[[Category: cytochrome c]]
[[Category: cytochrome c]]
[[Category: organic solvent]]
[[Category: organic solvent]]


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Revision as of 14:43, 21 February 2008

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1lc2

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Solution Structure Of Reduced Horse Heart Cytochrome c in 30% Acetonitrile Solution, NMR 30 Structures

OverviewOverview

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.

About this StructureAbout this Structure

1LC2 is a Single protein structure of sequence from Equus caballus with as ligand. Full crystallographic 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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