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Roman A. Laskowski
Researcher at European Bioinformatics Institute
Publications - 120
Citations - 50545
Roman A. Laskowski is an academic researcher from European Bioinformatics Institute. The author has contributed to research in topics: Protein structure & Protein Data Bank. The author has an hindex of 52, co-authored 119 publications receiving 45734 citations. Previous affiliations of Roman A. Laskowski include Birkbeck, University of London & Wellcome Trust.
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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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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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LigPlot+: multiple ligand-protein interaction diagrams for drug discovery.
TL;DR: A graphical system for automatically generating multiple 2D diagrams of ligand-protein interactions from 3D coordinates that facilitates popular research tasks, such as analyzing a series of small molecules binding to the same protein target, a single ligand binding to homologous proteins, or the completely general case where both protein and ligand change.
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Main-chain bond lengths and bond angles in protein structures.
TL;DR: The main-chain bond lengths and bond angles of protein structures are analysed as a function of resolution and differences in means are found to be highly statistically significant, suggesting that the different target values used by the different methods leave their imprint on the structures they refine.