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.
Disease
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Structural highlights
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