A ‘periodic table’ for protein structures View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2002-04

AUTHORS

William R. Taylor

ABSTRACT

Current structural genomics programs aim systematically to determine the structures of all proteins coded in both human and other genomes, providing a complete picture of the number and variety of protein structures that exist. In the past, estimates have been made on the basis of the incomplete sample of structures currently known. These estimates have varied greatly (between 1,000 and 10,000; see for example refs 1 and 2), partly because of limited sample size but also owing to the difficulties of distinguishing one structure from another. This distinction is usually topological, based on the fold of the protein; however, in strict topological terms (neglecting to consider intra-chain cross-links), protein chains are open strings and hence are all identical. To avoid this trivial result, topologies are determined by considering secondary links in the form of intra-chain hydrogen bonds (secondary structure) and tertiary links formed by the packing of secondary structures. However, small additions to or loss of structure can make large changes to these perceived topologies and such subjective solutions are neither robust nor amenable to automation. Here I formalize both secondary and tertiary links to allow the rigorous and automatic definition of protein topology. More... »

PAGES

657-660

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/416657a

DOI

http://dx.doi.org/10.1038/416657a

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1032338137

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/11948354


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