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Single‐Molecule FRET of Membrane Transport Proteins
Author(s) -
Bartels Kim,
LasitzaMale Tanya,
Hofmann Hagen,
Löw Christian
Publication year - 2021
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.202100106
Subject(s) - förster resonance energy transfer , single molecule fret , biomolecule , membrane transport protein , structural biology , flexibility (engineering) , nanotechnology , membrane biology , membrane transport , function (biology) , membrane protein , membrane , biophysics , biology , materials science , physics , biochemistry , microbiology and biotechnology , statistics , mathematics , quantum mechanics , fluorescence
Uncovering the structure and function of biomolecules is a fundamental goal in structural biology. Membrane‐embedded transport proteins are ubiquitous in all kingdoms of life. Despite structural flexibility, their mechanisms are typically studied by ensemble biochemical methods or by static high‐resolution structures, which complicate a detailed understanding of their dynamics. Here, we review the recent progress of single molecule Förster Resonance Energy Transfer (smFRET) in determining mechanisms and timescales of substrate transport across membranes. These studies do not only demonstrate the versatility and suitability of state‐of‐the‐art smFRET tools for studying membrane transport proteins but they also highlight the importance of membrane mimicking environments in preserving the function of these proteins. The current achievements advance our understanding of transport mechanisms and have the potential to facilitate future progress in drug design.