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The endogen steroid hormone 17b-estradiol is a central player in a wide range of physiologic, behavioral processes and diseases in vertebrates. As a consequence, it is a main target for molecular design and drug discovery efforts in medicine and environmental sciences, which requires in-depth knowledge of protein-ligand binding processes. This work develops a bioinformatic framework based on local and global structure similarity for the characterization of E2-protein interactions in all 35 publicly available three-dimensional structures of estradiol-protein complexes. Subsequently, it uses gained data to identify four geometrically conserved estradiol binding residue motifs, against which the Protein Data Bank is queried. As result of this database query, 15 hits present in seven protein structures are found. Five of these structures do not contain E2 as ligand and had thus not been included in this work’s initial data set. One of these newly detected structures is structurally and functionally dissimilar, as well as evolutionarily distant from all other proteins analyzed in this work. Nevertheless, the ability of this protein to actually bind estradiol must be further analyzed. Finally, geometrically conserved E2-protein interactions are identified and a new research direction using these conserved interaction ensembles for the detection of novel estradiol targets is proposed.
The Blockchain is a technology which has the capabilities to change the way, the world operates. As promising as this may be, there are still many challenges which do not exist or are way simpler to solve in conventional software solutions. Services which are offered over the blockchain suffer from so called Block-confirmation-times where the customer simply has to wait till the transaction is confirmed. In this paper possible solutions to that problem will be examined and challenges that arise from the specific criteria of the Ethereum Blockchain will be analyzed.
Brassica oleracea like all crucifers plants have a defense mechanism against natural enemies, which are chemical compounds formed form the enzymatic degradation of glucosinolates. In the presence of epithiospecifier proteins (ESP), the hydrolysis of glucosinolates will form epithionitriles or nitriles depending on the glucosinolate structure, This research proved that three predicted sequences (ESP) taken from NCBI database has a role in the enzymatic hydrolysis of glucosinolates in Brassica oleracea.