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

•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...

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Published inCurrent opinion in structural biology Vol. 57; pp. 93 - 102
Main Authors Heath, George R, Scheuring, Simon
Format Journal Article
LanguageEnglish
Published England Elsevier Ltd 01.08.2019
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Abstract •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.
AbstractList 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 towards 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.
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.
•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.
Author Scheuring, Simon
Heath, George R
AuthorAffiliation 2 Weill Cornell Medicine, Department of Physiology and Biophysics, 1300 York Avenue, New York, NY-10065, USA
1 Weill Cornell Medicine, Department of Anesthesiology, 1300 York Avenue, New York, NY-10065, USA
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  givenname: Simon
  surname: Scheuring
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  email: sis2019@med.cornell.edu
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BackLink https://www.ncbi.nlm.nih.gov/pubmed/30878714$$D View this record in MEDLINE/PubMed
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Snippet •HS-AFM detects conformational changes of unlabeled membrane proteins.•In situ responses to pH, ligands, temperature and light can be visualized.•Developments...
Recent advances in high-speed atomic force microscopy (HS-AFM) have made it possible to study the conformational dynamics of single unlabeled transmembrane...
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Title Advances in high-speed atomic force microscopy (HS-AFM) reveal dynamics of transmembrane channels and transporters
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https://www.ncbi.nlm.nih.gov/pubmed/30878714
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