Advances in high-speed atomic force microscopy (HS-AFM) reveal dynamics of transmembrane channels and transporters

• Published in: Current opinion in structural biology Vol. 57; pp. 93 - 102
• Main Authors: Heath, George R, Scheuring, Simon
• Format: Journal Article
• Language: English
• Published: England Elsevier Ltd 01.08.2019
• ISSN: 0959-440X; 1879-033X
• DOI: 10.1016/j.sbi.2019.02.008

•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.