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Protein-protein docking is the prediction of the structure of the complex, given the structures of the individual proteins.
The prediction of the structure of biological macromolecules at the atomic level and the design of new meta-stable structures and secondary interactions are critical tests of our understanding of the structures and the inter-atomic forces that underlie molecular biology.
Gray is the original developer of RosettaDock, a multi-scale algorithm and leading tool for the prediction of the structure of protein complexes from their constituent proteins.
This allowed the identification of the nature and orientation of sequences present at the breakpoint relative to the parental chromosome sequences allowing prediction of the structure of the resulting rearranged chromosomes.
Otherwise, it makes an ab initio prediction of the structure of the protein.
Furthermore, the prediction of the structure of the upstream coil bordered by two cysteines remains to be addressed.
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Topology-based models with smooth energy landscapes give reasonable predictions of the structure of the transition state ensemble, but do not have the kinetic or thermodynamic cooperativity exhibited by two-state proteins.
The complete model is demonstrated to yield plausible predictions of the structure of both the near-field non-reacting and subsonic combusting zones within wind blown fires, and to provide realistic predictions of flame lift-off heights, mean temperatures, trajectories and the radiation fluxes received about a number of field-scale jet fires.
The prediction of the structures of proteins without detectable sequence similarity to any protein of known structure remains an outstanding scientific challenge.
Our data resources on pig-expressed genes have greatly contributed to prediction of the structures of genes on the draft sequence of the pig genome.
In the past, the factor that has limited the success of this type of prediction is a detailed knowledge of the structure of the network.
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