Exemplartyp | Aktuellt bibliotek | Avdelning | Hyllsignatur | Status | Förfallodatum | Streckkod | Exemplarreservationer | |
---|---|---|---|---|---|---|---|---|
Bok | PRV - Biblioteket Stockholm | . | KEM.BIBL (Liknande titlar(Öppnas nedan)) | Tillgänglig | 20176778231F5 |
Includes bibliographical references and indexes.
Designing a diverse high-quality library for crystallography-based FBDD screening -- Preparation of protein samples for NMR structure, function, and small-molecule screening studies -- Key factors for successful generation of protein-fragment structures requirement on protein, crystals, and technology -- Predicting the success of fragment screening by X-ray crystallography -- Fragment screening of stabilized G-protein-coupled receptors using biophysical methods -- Using computational techniques in fragment-based drug discovery -- How to avoid rediscovering the known -- From experimental design to validated hits a comprehensive walk-through of fragment lead identification using surface plasmon resonance -- Practical aspects of NMR-based fragment screening -- Binding site identification and structure determination of protein-ligand complexes by NMR a semiautomated approach -- Protein thermal shifts to identify low molecular weight fragments -- HTS reporter displacement assay for fragment screening and fragment evolution toward leads with optimized binding kinetics, binding selectivity, and thermodynamic signature -- Fragment screening purely with protein crystallography -- Computational approach to de novo discovery of fragment binding for novel protein states -- Lead generation and examples opinion regarding how to follow up hits -- Medicinal chemistry inspired fragment-based drug discovery -- Effective progression of nuclear magnetic resonance-detected fragment hits -- Advancing fragment binders to lead-like compounds using ligand and protein-based NMR spectroscopy -- Electron density guided fragment-based drug design--a lead generation example -- Experiences in fragment-based lead discovery -- Fragment screening of infectious disease targets in a structural genomics environment.
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