Avidin: Difference between revisions
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The binding affinity of biotin for the avidin <scene name='41/410356/Cv/10'>receptors</scene> is very hight or in other words, the strength of the interations between the biotin and the avidin receptors is so strong that washing the biotin-avidin complex is not enough to remove the ligand from its pocket. This is not even possible by adding more biotin molecules to the system avidin-biotin. Once a <scene name='41/410356/Cv/12'>biotin has bound a pocket in the avidin</scene>, it is almost imposible to remove it in a biologica system! | The binding affinity of biotin for the avidin <scene name='41/410356/Cv/10'>receptors</scene> is very hight or in other words, the strength of the interations between the biotin and the avidin receptors is so strong that washing the biotin-avidin complex is not enough to remove the ligand from its pocket. This is not even possible by adding more biotin molecules to the system avidin-biotin. Once a <scene name='41/410356/Cv/12'>biotin has bound a pocket in the avidin</scene>, it is almost imposible to remove it in a biologica system! | ||
Each monomer is an eight-stranded antiparallel <scene name=' | Each monomer is an eight-stranded antiparallel <scene name='41/410356/Cv/13'>beta-barrel</scene>. Binding of biotin involves a highly stabilized network of polar and hydrophobic interactions. | ||
The presence of additional hydrophobic and hydrophilic groups in the binding site of avidin may account for its higher affinity constant. | The presence of additional hydrophobic and hydrophilic groups in the binding site of avidin may account for its higher affinity constant. | ||