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000009747 084__ $$2WoS$$aBiochemistry & Molecular Biology
000009747 1001_ $$0P:(DE-Juel1)VDB630$$aHoffmann, S.$$b0$$uFZJ
000009747 245__ $$aCompetitively selected protein ligands pay their increase in specificity by a decrease in affinity
000009747 260__ $$aCambridge$$bRoyal Society of Chemistry$$c2010
000009747 300__ $$a126 - 133
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000009747 440_0 $$020661$$aMolecular BioSystems$$v6$$x1742-206X$$y1
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000009747 520__ $$aProtein-ligand interactions characterise and govern the current state and fate of a living cell. The specificity of proteins is mainly determined by the relative affinities to each potential ligand. To investigate the consequences and potentials of ligands with increased specificity in comparison with ligands optimised solely for affinity, it was necessary to identify ligands that are optimised towards specificity instead of a barely optimised affinity to a given target. In the presented example, a modified phage display screening procedure yielded specific ligands for the LckSH3 domain. We found that increased specificity of one of the hereby obtained ligands for LckSH3 is achieved at the cost of a slightly reduced affinity to LckSH3 and a drastically reduced affinity to other SH3 domains. A surface plasmon resonance experiment simulating in vivo-like realistic competitive binding conditions exerted enhanced binding behaviour of the specific ligand under these binding conditions. The experimental data, together with a mathematical model describing the complex experimental situation, and theoretical considerations lead to the conclusion that increased specificity is achieved at the cost of reduced affinity, but after all, it pays if the ligand is applied under realistic, i.e. competitive, conditions.
000009747 536__ $$0G:(DE-Juel1)FUEK409$$2G:(DE-HGF)$$aFunktion und Dysfunktion des Nervensystems$$cP33$$x0
000009747 536__ $$0G:(DE-Juel1)FUEK505$$aBioSoft: Makromolekulare Systeme und biologische Informationsverarbeitung$$cP45$$x1
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000009747 650_2 $$2MeSH$$aBinding Sites: genetics
000009747 650_2 $$2MeSH$$aBinding Sites: physiology
000009747 650_2 $$2MeSH$$aLigands
000009747 650_2 $$2MeSH$$aPeptide Library
000009747 650_2 $$2MeSH$$aProtein Binding
000009747 650_2 $$2MeSH$$aProteins: chemistry
000009747 650_2 $$2MeSH$$aProteins: metabolism
000009747 650_2 $$2MeSH$$aSurface Plasmon Resonance
000009747 650_2 $$2MeSH$$asrc Homology Domains: genetics
000009747 650_2 $$2MeSH$$asrc Homology Domains: physiology
000009747 650_7 $$00$$2NLM Chemicals$$aLigands
000009747 650_7 $$00$$2NLM Chemicals$$aPeptide Library
000009747 650_7 $$00$$2NLM Chemicals$$aProteins
000009747 650_7 $$2WoSType$$aJ
000009747 7001_ $$0P:(DE-Juel1)VDB65869$$aFunke, S. A.$$b1$$uFZJ
000009747 7001_ $$0P:(DE-HGF)0$$aWiesehan, K.$$b2
000009747 7001_ $$0P:(DE-Juel1)VDB92202$$aMoedder, S.$$b3$$uFZJ
000009747 7001_ $$0P:(DE-Juel1)VDB89237$$aGlück, J.M.$$b4$$uFZJ
000009747 7001_ $$0P:(DE-HGF)0$$aFeuerstein, S.E.$$b5
000009747 7001_ $$0P:(DE-HGF)0$$aGerdts, J.$$b6
000009747 7001_ $$0P:(DE-Juel1)VDB92205$$aMoetter, J.$$b7$$uFZJ
000009747 7001_ $$0P:(DE-Juel1)132029$$aWillbold, D.$$b8$$uFZJ
000009747 773__ $$0PERI:(DE-600)2188635-0$$a10.1039/b910945e$$gVol. 6, p. 126 - 133$$p126 - 133$$q6<126 - 133$$tMolecular BioSystems$$v6$$x1742-206X$$y2010
000009747 8567_ $$uhttp://dx.doi.org/10.1039/b910945e
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