Direct Observation of the Reversible Two-State Unfolding and Refolding of an α/β Protein by Single-Molecule Atomic Force Microscopy

Direct Observation of the Reversible Two-State Unfolding and Refolding of an α/β Protein by Single-Molecule Atomic Force Microscopy

Directly observing protein folding in real time using atomic force microscopy (AFM) is challenging. Here the use of AFM to directly monitor the folding of an α/β protein, NuG2, by using low‐drift AFM cantilevers is demonstrated. At slow pulling speeds (

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Veröffentlicht in:Angewandte Chemie International Edition 2015-08, Vol.54 (34), p.9921-9925
Hauptverfasser: He, Chengzhi, Hu, Chunguang, Hu, Xiaodong, Hu, Xiaotang, Xiao, Adam, Perkins, Thomas T., Li, Hongbin
Format: Artikel
Sprache:eng
Schlagworte:
Atomic force microscopy
Elastomers
Equilibrium
Fluctuation
fluctuation theorem
Folding
force spectroscopy
Free energy
Microscopes
Microscopy
Microscopy, Atomic Force
Monitors
Protein folding
Protein Refolding
Protein Structure, Secondary
Protein Unfolding
Proteins
Proteins - chemistry
Real time
single-molecule studies
Stability
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Beschreibung
Zusammenfassung:Directly observing protein folding in real time using atomic force microscopy (AFM) is challenging. Here the use of AFM to directly monitor the folding of an α/β protein, NuG2, by using low‐drift AFM cantilevers is demonstrated. At slow pulling speeds (
ISSN:1433-7851
1521-3773
DOI:10.1002/anie.201502938