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Heath, George R; Scheuring, Simon
Current opinion in structural biology, 08/2019, Letnik: 57Journal Article
•HS-AFM detects conformational changes of unlabeled membrane proteins.•In situ responses to pH, ligands, temperature and light can be visualized.•Developments in techniques now allow microsecond temporal resolution. Recent advances in high-speed atomic force microscopy (HS-AFM) have made it possible to study the conformational dynamics of single unlabeled transmembrane channels and transporters. Improving environmental control with the integration of a non-disturbing buffer exchange system, which in turn allows the gradual change of conditions during HS-AFM operation, has provided a breakthrough toward the performance of structural titration experiments. Further advancements in temporal resolution with the use of line scanning and height spectroscopy techniques show how high-speed atomic force microscopy can measure millisecond to microsecond dynamics, pushing this method beyond current spatial and temporal limits offered by less direct techniques.
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