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William R. Taylor
Researcher at Francis Crick Institute
Publications - 89
Citations - 17878
William R. Taylor is an academic researcher from Francis Crick Institute. The author has contributed to research in topics: Protein structure & Structural alignment. The author has an hindex of 42, co-authored 89 publications receiving 16840 citations. Previous affiliations of William R. Taylor include Lincoln's Inn & Tokyo Institute of Technology.
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The rapid generation of mutation data matrices from protein sequences
TL;DR: An efficient means for generating mutation data matrices from large numbers of protein sequences is presented, by means of an approximate peptide-based sequence comparison algorithm, which is fast enough to process the entire SWISS-PROT databank in 20 h on a Sun SPARCstation 1, and is fastenough to generate a matrix from a specific family or class of proteins in minutes.
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A new approach to protein fold recognition.
TL;DR: A new approach to fold recognition, whereby sequences are fitted directly onto the backbone coordinates of known protein structures, using a given sequence as a guide for the matching of sequences to backbone coordinates.
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Role of the polycomb protein EED in the propagation of repressive histone marks
Raphaël Margueron,Neil Justin,Katsuhito Ohno,Miriam Sharpe,Jinsook Son,William J. Drury,Philipp Voigt,Stephen R. Martin,William R. Taylor,Valeria De Marco,Vincenzo Pirrotta,Danny Reinberg,Steven J. Gamblin +12 more
TL;DR: It is shown that the carboxy-terminal domain of EED specifically binds to histone tails carrying trimethyl-lysine residues associated with repressive chromatin marks, and that this leads to the allosteric activation of the methyltransferase activity of PRC2.
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A model recognition approach to the prediction of all-helical membrane protein structure and topology.
TL;DR: The method employs a set of statistical tables (log likelihoods) complied from well-characterized membrane protein data, and a novel dynamic programming algorithm to recognize membrane topology models by expectation maximization.
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The classification of amino acid conservation
TL;DR: A classification of amino acid type is described which is based on a synthesis of physico-chemical and mutation data in the form of a Venn diagram from which sub-sets are derived that include groups of amino acids likely to be conserved for similar structural reasons.