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New page: left|200px<br /><applet load="1jvl" size="450" color="white" frame="true" align="right" spinBox="true" caption="1jvl, resolution 2.0Å" /> '''Azurin dimer, covalen...
 
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[[Image:1jvl.gif|left|200px]]<br /><applet load="1jvl" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1jvl.gif|left|200px]]<br /><applet load="1jvl" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1jvl, resolution 2.0&Aring;" />
caption="1jvl, resolution 2.0&Aring;" />
'''Azurin dimer, covalently crosslinked through bis-maleimidomethylether'''<br />
'''Azurin dimer, covalently crosslinked through bis-maleimidomethylether'''<br />


==Overview==
==Overview==
The transfer of electrons between proteins is an essential step in, biological energy production. Two protein redox partners are often, artificially crosslinked to investigate the poorly understood mechanism by, which they interact. To better understand the effect of crosslinking on, electron transfer rates, we have constructed dimers of azurin by, crosslinking the monomers. The measured electron exchange rates, combined, with crystal structures of the dimers, demonstrate that the length of the, linker can have a dramatic effect on the structure of the dimer and the, electron transfer rate. The presence of ordered water molecules in the, protein-protein interface may considerably influence the electronic, coupling between redox centers.
The transfer of electrons between proteins is an essential step in biological energy production. Two protein redox partners are often artificially crosslinked to investigate the poorly understood mechanism by which they interact. To better understand the effect of crosslinking on electron transfer rates, we have constructed dimers of azurin by crosslinking the monomers. The measured electron exchange rates, combined with crystal structures of the dimers, demonstrate that the length of the linker can have a dramatic effect on the structure of the dimer and the electron transfer rate. The presence of ordered water molecules in the protein-protein interface may considerably influence the electronic coupling between redox centers.


==About this Structure==
==About this Structure==
1JVL is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa] with CU, NI, 144 and OPP as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1JVL OCA].  
1JVL is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa] with <scene name='pdbligand=CU:'>CU</scene>, <scene name='pdbligand=NI:'>NI</scene>, <scene name='pdbligand=144:'>144</scene> and <scene name='pdbligand=OPP:'>OPP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JVL OCA].  


==Reference==
==Reference==
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[[Category: Pseudomonas aeruginosa]]
[[Category: Pseudomonas aeruginosa]]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Amsterdam, I.M.C.van.]]
[[Category: Amsterdam, I M.C van.]]
[[Category: Canters, G.W.]]
[[Category: Canters, G W.]]
[[Category: Cavazzini, D.]]
[[Category: Cavazzini, D.]]
[[Category: Einsle, O.]]
[[Category: Einsle, O.]]
[[Category: Merli, A.]]
[[Category: Merli, A.]]
[[Category: Messerschmidt, A.]]
[[Category: Messerschmidt, A.]]
[[Category: Rossi, G.L.]]
[[Category: Rossi, G L.]]
[[Category: Ubbink, M.]]
[[Category: Ubbink, M.]]
[[Category: 144]]
[[Category: 144]]
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[[Category: electron transfer]]
[[Category: electron transfer]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 18:36:41 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:27:13 2008''