User:Noam Gonen/Avidin
From Proteopedia
(Difference between revisions)
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== Structure == | == Structure == | ||
The tetrameric protein contains four identical subunits (homotetramer), each of which can bind to biotin (Vitamin B7, vitamin H) with a high degree of affinity and specificity. The dissociation constant of avidin is measured to be KD ≈ 10−15 M, making it one of the strongest known non-covalent bonds[2].The overall fold of the avidin monomer is constructed of eight antiparallel β-strands which form classical β-barrel. | The tetrameric protein contains four identical subunits (homotetramer), each of which can bind to biotin (Vitamin B7, vitamin H) with a high degree of affinity and specificity. The dissociation constant of avidin is measured to be KD ≈ 10−15 M, making it one of the strongest known non-covalent bonds[2].The overall fold of the avidin monomer is constructed of eight antiparallel β-strands which form classical β-barrel. | ||
| - | == | + | == Monomer- monomer interaction == |
| - | + | '''Interaction 1-2''' | |
== Relevance == | == Relevance == | ||
Revision as of 15:31, 17 January 2015
INTRODUCTION
Avidin is a tetrameric or dimeric[1] biotin-binding protein produced in the oviducts of birds, reptiles and amphibians and deposited in the whites of their eggs.
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