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Biomolecules are able to specifically recognize and bind their corresponding partner with high efficiency. This process plays a pivotal role in biology, physiology and medicine (e.g., in the immune system, cellular adhesion or inter- and intracellular signaling). From the chemical point of view bio-recognition can be described as a combination of non-covalent weak interactions including electrostatic (ionic), hydrophobic, and van der Waals interactions as well as hydrogen bonding. Furthermore, steric aspects, especially the complementary structure of the two binding partners, are highly relevant for complex formation and stability. Taken together all these aspects determine both, the strength and the characteristic lifetime of the bond. In addition to bulk techniques like nuclear magnetic resonance, surface plasmon resonance, quartz crystal microbalance, and other analytical and biochemical methods single molecule approaches have been established. They allow following transient phenomena like short-lived receptor-ligand intermediate states, rare events, or population heterogeneity, which are otherwise not accessible. For the determination of single receptor ligand interactions, apart from bio-membrane force probe, and optical and magnetic tweezers, atomic force microscopy (AFM) based molecular recognition forces spectroscopy (MRFS) offers the most versatile approach to explore forces during the bio-recognition processes at the molecular level
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