K
Kathryn Loving
Researcher at Schrödinger
Publications - 5
Citations - 477
Kathryn Loving is an academic researcher from Schrödinger. The author has contributed to research in topics: Docking (molecular) & Protein structure prediction. The author has an hindex of 4, co-authored 5 publications receiving 392 citations.
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Applying physics-based scoring to calculate free energies of binding for single amino acid mutations in protein-protein complexes.
TL;DR: This work compares predictions to experimental data for a set of 418 single residue mutations in 21 targets and finds that the MM-GBSA model, on average, performs well at scoring these single protein residue mutations.
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Energetic analysis of fragment docking and application to structure-based pharmacophore hypothesis generation.
TL;DR: A method to use the energetically selected sites from fragment docking to develop a pharmacophore hypothesis that can be used in virtual database screening to retrieve diverse compounds is described and finds that this method produces viable hypotheses that are consistent with known active compounds.
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Computational Approaches for Fragment-Based and De Novo Design
TL;DR: Recent research results suggesting that computational tools applied to fragment-based discovery and de novo design can have a greater impact on the discovery process when coupled with the right experiments are presented.
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Structure-based druggability assessment of the mammalian structural proteome with inclusion of light protein flexibility.
TL;DR: An approach is applied that uses protein modeling in concert with druggability estimation to account for light protein backbone movement and protein side-chain flexibility in protein binding sites and results in identification of 69 proteins with potential druggable cryptic pockets.
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Generation of structure-based pharmacophores using energetic analysis – application on fragment docking
TL;DR: It is shown that the most energetically favourable pharmacophore sites are consistent with features from known tight binding compounds, which are able to recover known active compounds from a database screen and retrieving diverse compounds that are not biased by the co-crystallized ligand.