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Introduction
The atomic force microscope (AFM) 1 is well known for its high imaging resolution even at ambient environment and room temperature. Besides that, it can be used to measure forces, accurately. Its force resolution at room temperature is high enough to measure forces as small as weak bindings between biological molecules 2, 3, 4, 5, 6. Those abilities make the AFM, especially force distance based AFM methods a valuable tool to investigate biological functions 7, 8 .
For biological processes weak interactions play a crucial role. Usually, ligand-receptor type complexes of proteins (e.g. antibodies, enzymes) and/or other organic biomolecules (e.g. vitamins, hormones) are formed. The lifetime and stability of such formed complexes is optimized for its biological function. Therefore measuring that weak interaction of proteins is important to understand its function.
Here, we show how the Keysight Technologies, Inc. 7500 AFM can be utilized to improve the molecular understanding of complex biological systems. In particular we show how interactions between proteins can be studied by Single Molecule Force Spectroscopy (SMFS), yielding the energy landscape.
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