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- W156778305 abstract "Abstract Proteins are built from basic structural elements and their systematic characterization is of interest. Searching for recurring patterns in protein contact maps, we found several network motifs, patterns that occur more frequently in experimentally determined protein contact maps than in randomized contact maps with the same properties. Some of these network motifs correspond to sub-structures of alpha helices, including topologies not previously recognized in this context. Other motifs characterize beta-sheets, again some of which appear to be novel. This topological characterization of patterns serves as a tool to characterize proteins, and to reveal a high detailed differences map for comparing protein structures solved by X-ray crystallography, NMR and molecular dynamics (MD) simulations. Both NMR and MD show small but consistent differences from the crystal structures of the same proteins, possibly due to the pair-wise energy functions used. Network motifs analysis can serve as a base for many-body energy statistical energy potential, and suggests a dictionary of basic elements of which protein secondary structure is made." @default.
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- W156778305 date "2008-01-04" @default.
- W156778305 modified "2023-10-16" @default.
- W156778305 title "Understanding Hydrogen-Bond Patterns in Proteins using a Novel Statistical Model" @default.
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- W156778305 doi "https://doi.org/10.1038/npre.2008.1490.1" @default.
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