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By Vivekananda Kendra -

SHAKTI SURABHI BIO power PLANT on your again backyard

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Zhang and Skolnick developed TASSER, a threading template assembly/refinement approach, for ab initio prediction of protein structures (Zhang and Skolnick, 2004). The test of TASSER on a comprehensive benchmark set of 1489 single-domain proteins in the Protein Data Bank (PDB) with length below 200 residues showed that 990 targets could be folded by TASSER with an RMSD < ˚ in at least one of the top five models. 5 A TASSER are derived in a different way than in Rosetta. 7 residues on average) than the segments used by Rosetta (which are 3–9 residues).

This technique has been applied in solving the structures of large biological machines/macromolecular complexes, such as viruses, ion channels, ribosomes, and proteasomes. In cases where no experimental high-resolution structures are available, computational models of the individual proteins may instead be used in fitting. In addition, intermediateresolution cryo-EM density maps are helpful for improving the accuracy of comparative protein structure modeling in those cases for which no template for modeling can be found by a sequence-based search or a threading method.

The combinatorial assembly of domains is formulated as the problem of finding the spanning tree in a graph (where each substructure is a vertex, and an SVNY330-Xu-Vol-I November 2, 2006 16:58 1. A Historical Perspective and Overview 25 edge between two vertices presents the interaction of the two substructures), and a heuristic polynomial solution to this computational hard problem has been provided. Jones et al. , domain docking and microdomain folding, to model complete chains of selected CASP6 targets.

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