Receptor―Ligand Interactions: Binding Affinities Studied by Single-Molecule and Super-Resolution Microscopy on Intact Cells
In: ChemPhysChem (Print), Jg. 15 (2014), Heft 4, S. 671-676
Online
academicJournal
- print, 50 ref
Zugriff:
Protein―ligand interactions play an important role in many biological processes. Notably, membrane receptors are the starting point for a huge variety of cellular signal transduction pathways. Quantifying the binding affinity of a ligand for its transmembrane receptor is of great importance as it provides information on the potency of the ligand. We developed a new experimental procedure to determine binding affinities of ligands for their membrane receptors directly on intact single cells using super-resolution imaging. Dissociation constants were determined by titrating fluorophore-labelled ligand against cells expressing the target protein and applying single-molecule imaging.
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Receptor―Ligand Interactions: Binding Affinities Studied by Single-Molecule and Super-Resolution Microscopy on Intact Cells
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Autor/in / Beteiligte Person: | DIETZ, Marina S ; FRICKE, Franziska ; KRÜGER, Carmen L ; NIEMANN, Hartmut H ; HEILEMANN, Mike |
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Zeitschrift: | ChemPhysChem (Print), Jg. 15 (2014), Heft 4, S. 671-676 |
Veröffentlichung: | Weinheim: Wiley, 2014 |
Medientyp: | academicJournal |
Umfang: | print, 50 ref |
ISSN: | 1439-4235 (print) |
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