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Its core structure consists of eight multicomponent protein complexes, most of which are conserved in all eukaryotes.
The core structure consists of a rigid skeleton containing two different types of receptor site in a single molecular motif designed to combine a transition metal ion [Ir III)] and a lanthanide ion [Ln III)] in different binding sites at either end of fully conjugated bridge to facilitate d → f energy-transfer following photoexcitation of the Ir III -based antenna unIr III -based
This core structure consists of 14 copies of each of the proteins and forms two layers, inserting in the inner and outer membrane, respectively [ 45].
It is generally agreed that the centrosome core structure consists of permanently associated centrosome proteins that remain after treatment of the centrosome complex with microtubule depolymerizing agents such as cold, nocodazole, colchicine derivatives, and others.
Integrons are mobile DNA elements, and their core structure consists of a gene that codes for an integrase, IntI, and a proximal primary recombination sequence called attI site that allow bacteria to capture and express gene cassettes (Mazel 2006; Boucher et al. 2007).
Their core structure consists of four beta strands, crosslinked by four disulfide bridges [ 5, 6], creating a structure enabling the self-assembly at a hydrophilic/hydrophobic interface between the hydrophilic cell wall and a hydrophobic environment (such as air or the hydrophobic surface of living and non-living material).
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Enediyne natural products are extremely potent antitumor antibiotics with a remarkable core structure consisting of two acetylenic groups conjugated to a double bond within either a 9‐ or 10‐membered ring.
Furthermore, a coated core structure consisting of an internal graphitized carbon sphere and an external MnO2 layer is successfully synthesized, which not only possesses high surface area and hierarchical porosity, but also has improved electrical conductivity.
The five p85 isoforms have a common core structure consisting of a p110-binding domain surrounded by two Src-homology-2 domains (SH2).
The hotdog-fold thioesterases possess a characteristic core structure consisting of a 5-turn α-helix cradled by a curved, 5-stranded antiparallel β-sheet.
The members of this family are proteins of approximately one hundred aminoacids with four conserved cysteine residues that coordinate the 2[Fe-S] cluster and have a general core structure consisting of beta(2 -alpha-beta(2 -alpha-beta
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