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• W1968002829 abstract "A new, automated, knowledge-based method for the construction of three-dimensional models of proteins is described. Geometric restraints on target structures are calculated from a consideration of homologous template structures and the wider knowledge base of unrelated protein structures. Three-dimensional structures are calculated from initial partly folded states by high-temperature molecular dynamics simulations followed slow cooling of the system (simulated annealing) using nonphysical potentials. Three-dimensional models for the biotinylated domain from the pyruvate carboxylase of yeast and the lipoylated H-protein from the glycine cleavage system of pea leaf were constructed, based on the known structures of two lipoylated domains of 2-oxo acid dehydrogenase multienzyme complexes. Despite their weak sequence similarity, the three proteins are predicted to have similar three-dimensional structures, representative of a new protein module. Implications for the mechanisms of posttranslational modification of these proteins and their catalytic function are discussed." @default.
• W1968002829 created "2016-06-24" @default.
• W1968002829 creator A5029547053 @default.
• W1968002829 creator A5060338852 @default.
• W1968002829 date "1993-04-01" @default.
• W1968002829 modified "2023-10-12" @default.
• W1968002829 title "Prediction of the three-dimensional structures of the biotinylated domain from yeast pyruvate carboxylase and of the lipoylated H-protein from the pea leaf glycine cleavage system: A new automated method for the prediction of protein tertiary structure" @default.
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• W1968002829 doi "https://doi.org/10.1002/pro.5560020413" @default.
• W1968002829 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2142356" @default.
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