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Molecular Interaction Analysis for Discovery of Drugs Targeting Enzymes and for Resolving Biological Function
Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC, Biochemistry.
2015 (English)In: Multifaceted Roles Of Crystallography In Modern Drug Discovery / [ed] Scapin, G; Patel, D; Arnold, E, 2015, p. 223-240Conference paper, Published paper (Refereed)
Abstract [en]

Analysis of molecular interactions using surface plasmon resonance (SPR) biosensor technology has become a powerful tool for discovery of drugs targeting enzymes and resolving biological function. A major advantage of this technology over other methods for interaction analysis is that it can provide the kinetic details of interactions. This is a consequence of the time resolution of the analysis, which allows individual kinetic rate constants as well as affinities to be determined. A less commonly recognized feature of this technology is that it can reveal the characteristics of more complex mechanisms, e.g. involving multiple steps or conformations of the target or ligand, as well as the energetics, thermodynamics and forces involved.

Place, publisher, year, edition, pages
2015. p. 223-240
Series
NATO Science for Peace and Security Series A-Chemistry and Biology, ISSN 1874-6489
National Category
Pharmacology and Toxicology Medical Biotechnology (with a focus on Cell Biology (including Stem Cell Biology), Molecular Biology, Microbiology, Biochemistry or Biopharmacy)
Identifiers
URN: urn:nbn:se:uu:diva-309659DOI: 10.1007/978-94-017-9719-1_17ISI: 000380514200017ISBN: 9789401797245 (print)ISBN: 9789401797191 (print)ISBN: 9789401797184 (print)OAI: oai:DiVA.org:uu-309659DiVA, id: diva2:1052482
Conference
Conference of NATO-Advanced-Study-Institute on Crystallography in Drug Discovery - A Tool against CBRN Agents, MAY 30-JUN 08, 2014, Erice, ITALY
Available from: 2016-12-06 Created: 2016-12-06 Last updated: 2018-01-13Bibliographically approved

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Danielson, U. Helena

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