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Janet M. Thornton

Researcher at European Bioinformatics Institute

Publications -  552
Citations -  112339

Janet M. Thornton is an academic researcher from European Bioinformatics Institute. The author has contributed to research in topics: Protein structure & Structural genomics. The author has an hindex of 130, co-authored 539 publications receiving 105144 citations. Previous affiliations of Janet M. Thornton include Laboratory of Molecular Biology & University College London.

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PROCHECK: a program to check the stereochemical quality of protein structures

TL;DR: The PROCHECK suite of programs as mentioned in this paper provides a detailed check on the stereochemistry of a protein structure and provides an assessment of the overall quality of the structure as compared with well refined structures of the same resolution.
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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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AQUA and PROCHECK-NMR: programs for checking the quality of protein structures solved by NMR

TL;DR: The AQUA and PROCHECK-NMR programs provide a means of validating the geometry and restraint violations of an ensemble of protein structures solved by solution NMR, and their outputs include a detailed breakdown of the restraint violations.
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LIGPLOT: a program to generate schematic diagrams of protein-ligand interactions

TL;DR: The LIGPLOT program automatically generates schematic 2-D representations of protein-ligand complexes from standard Protein Data Bank file input giving a simple and informative representation of the intermolecular interactions and their strengths, including hydrogen bonds, hydrophobic interactions and atom accessibilities.
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CATH – a hierarchic classification of protein domain structures

TL;DR: Analysis of the structural families generated by CATH reveals the prominent features of protein structure space and a database of well-characterised protein structure families will facilitate the assignment of structure-function/evolution relationships to both known and newly determined protein structures.