Journal:JBSD:26

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<b>Molecular Tour</b><br>
<b>Molecular Tour</b><br>
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The binding mode of <scene name='Journal:JBSD:26/Cv/2'>erlotinib hydrochloride (ET)</scene>, a targeted anticancer drug, to <scene name='Journal:JBSD:26/Cv/5'>bovine serum albumin (BSA)</scene> was investigated through 1H NMR, spectroscopic, thermodynamic and molecular modeling methods. Each subdomain is marked with a different colour (<font color='red'><b>red for subdomain IA</b></font>; <span style="color:orange;background-color:black;font-weight:bold;">orange, IB</span>; <span style="color:dimgray;background-color:black;font-weight:bold;">grey, IIA</span>; <span style="color:yellow;background-color:black;font-weight:bold;">yellow, IIB</span>; <span style="color:lime;background-color:black;font-weight:bold;">green, IIIA</span>; <font color='darkmagenta'><b>darkmagenta, IIIB</b></font>). From these methods, the binding parameters, binding site, binding distance, and conformational changes were obtained. Site marker competitive experiments demonstrated that the <scene name='Journal:JBSD:26/Cv/6'>binding site was located in the hydrophobic pocket of site I (subdomain IIA)</scene>. The docking modeling agreed with the results of the fluorescence and displacement experiments.
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The binding mode of <scene name='Journal:JBSD:26/Cv/2'>erlotinib hydrochloride (ET)</scene>, a targeted anticancer drug, to <scene name='Journal:JBSD:26/Cv/8'>bovine serum albumin (BSA)</scene> was investigated through 1H NMR, spectroscopic, thermodynamic and molecular modeling methods. Each subdomain is marked with a different colour (<font color='red'><b>red for subdomain IA</b></font>; <span style="color:orange;background-color:black;font-weight:bold;">orange, IB</span>; <span style="color:cyan;background-color:black;font-weight:bold;">cyan, IIA</span>; <span style="color:yellow;background-color:black;font-weight:bold;">yellow, IIB</span>; <span style="color:lime;background-color:black;font-weight:bold;">green, IIIA</span>; <font color='darkmagenta'><b>darkmagenta, IIIB</b></font>). From these methods, the binding parameters, binding site, binding distance, and conformational changes were obtained. Site marker competitive experiments demonstrated that the <scene name='Journal:JBSD:26/Cv/6'>binding site was located in the hydrophobic pocket of site I (subdomain IIA)</scene>. The docking modeling agreed with the results of the fluorescence and displacement experiments.
</StructureSection>
</StructureSection>
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Revision as of 09:57, 3 September 2012

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Proteopedia Page Contributors and Editors (what is this?)

Alexander Berchansky, Jaime Prilusky

This page complements a publication in scientific journals and is one of the Proteopedia's Interactive 3D Complement pages. For aditional details please see I3DC.
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