Protein Data Bank

In the materials and methods section; ligand preparation, target protein identification and preparation, molecular descriptors calculation, ADME (Absorption, Distribution, Metabolism and Excretion) and TOPKAT (Toxicity Prediction by Komputer Assisted Technology) analysis were carried out according to the previously reported method as briefly stated below. Ligand preparation Chemical structures of the ligands i) asperyellone [CID101600052]; ii) asperenone [CID5368642]; iii) hydroasperyellone [CID561143];

structure of enzyme Plasmodium falciparum enzyme farnesyltransferase was not found available in Protein Data Bank (PDB) archive, therefore the structure was built using homology modeling method. In order to predict the structure of enzyme (PfFT), the sequence of enzyme IDs PF3D7_1242600 [alpha- subunit] and PF3D7_1147500 [beta subunit] were obtained from the web services (www.gene db.org), protein sequence data bank in swiss prot or uniprock KB (Q8IHP6), NCBI (AAW78025). The only sequence of the active site

How does zinc binds to proteins? Zinc coordinates proteins with four different surroundings with different roles: catalytic, co-catalytic, structural and interface. In many proteins Zn2+ ions also serve to correct polypeptide folding. Furthermore, zinc is a cofactor in all six enzyme classes. Zinc ions in protein interface may influence the formation of stable quaternary structures, as in the case of hexameric insulin, which is formed from three protein dimers and two Zn2+ ions. As has been said

characterizes the amino acid substitution (Ramensky et al. 2002). To determine the effect of variants on the protein secondary structure, inter chain contents, functional sites, and binding sites, Polyphen2.0 utilizes PDB (Protein Data Bank), DSSP (Dictionary of secondary structures in protein), and three-dimensional structure databases (Ramensky et al. 2002). We submitted the query in the form of the protein sequence with the mutational position of two amino

All four types ENRs require cofactors as an electron donor. FabI requires either of NADH or NADPH as cofactors.7 In the case of FabK, NADH is reductant, but acts indirectly by reducing the tightly bound Flavin cofactor.20 FabL uses NADPH as a cofactor,11 and FabV prefers NADH than NADPH.14 Therefore, we attempted to co-crystalize the vfFabV with its cofactor NADH. However, we were not able to succeed in observing interpretable electron density map for bound NADH. Until now, there are three available

results are found from each respective database. What’s the main reason for this discrepancy? Also, how many species represented in each and do each species appear to be equally represented by similar proportions of records? Provide a 3D image of this protein from H. sapiens, appropriately cited. ( 10 pts

acervulina remains unclear. Protein ubiquitination regulates cellular processes by influencing the stability and function of modified proteins. The ubiquitin (Ub) protein is highly conserved in all eukaryotes and composed of 76 amino acids. A single Ub protein or Ub oligomers can modify single or multiple lysine residues of the protein. Ubiquitin forms covalent chains through each of its seven lysine residues (Lys6, Lys11, Lys27,

erythrocytes (Homer et al., 2000). The 70 kDa heat-shock proteins (HSP-70s) are intracellular proteins found in all organisms. HSPs play important roles in cell proliferation and the control of cellular functions (Lindquist, 1986). Heat shock proteins (HSPs) are known as stress proteins because various forms of stress enhance their transcriptional activation and biosynthesis (Lindquist, 1986). As many bacteria and parasites produce HSP-70, the protein serves as an antigen for bacteria and parasitic pathogens

country with around 3 million people population. According to the most recent research data, 32% of the population lives below the national poverty level. As poverty levels have significantly decreased in recent years, malnutrition is still spread in Armenia, especially among young generation. Here are some facts which can clearly present the malnutrition situation in Republic of Armenia (20). 1. According to World Bank research, approximately 5.3 percent of Armenian children under the age of 5 are underweight

making up proteins-the nucleus, ribosomes, rough ER, and the golgi apparatus (Alberts, B. 2014). Proteins are very critical to cells, because they happen to be assembled by proteins, which in turn becomes major jobs that it does for