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

Overview

abstract

  • 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.

publication date

  • March 14, 2019

Research

keywords

  • Cell Membrane
  • Membrane Transport Proteins
  • Microscopy, Atomic Force

Identity

PubMed Central ID

  • PMC7216758

Scopus Document Identifier

  • 85062805426

Digital Object Identifier (DOI)

  • 10.1016/j.sbi.2019.02.008

PubMed ID

  • 30878714

Additional Document Info

volume

  • 57