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• W2115617617 abstract "Abstract In recent years, there have been significant advances in the field of computational protein design including the successful computational design of enzymes based on backbone scaffolds from experimentally solved structures. It is likely that large‐scale sampling of protein backbone conformations will become necessary as further progress is made on more complicated systems. Removing the constraint of having to use scaffolds based on known protein backbones is a potential method of solving the problem. With this application in mind, we describe a method to systematically construct a large number of de novo backbone structures from idealized topological forms in a top–down hierarchical approach. The structural properties of these novel backbone scaffolds were analyzed and compared with a set of high‐resolution experimental structures from the protein data bank (PDB). It was found that the Ramachandran plot distribution and relative γ‐ and β‐turn frequencies were similar to those found in the PDB. The de novo scaffolds were sequence designed with RosettaDesign, and the energy distributions and amino acid compositions were comparable with the results for redesigned experimentally solved backbones. Proteins 2010. © 2009 Wiley‐Liss, Inc." @default.
• W2115617617 created "2016-06-24" @default.
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• W2115617617 date "2009-12-16" @default.
• W2115617617 modified "2023-10-18" @default.
• W2115617617 title "<i>De novo</i> backbone scaffolds for protein design" @default.
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• W2115617617 doi "https://doi.org/10.1002/prot.22651" @default.
• W2115617617 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2841848" @default.
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