Optimizing 1‑μs-Resolution Single-Molecule Force Spectroscopy on a Commercial Atomic Force Microscope

Atomic force microscopy (AFM)-based single-molecule force spectroscopy (SMFS) is widely used to mechanically measure the folding and unfolding of proteins. However, the temporal resolution of a standard commercial cantilever is 50–1000 μs, masking rapid transitions and short-lived intermediates. Rec...

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Bibliographic Details
Published in:Nano letters 2015-10, Vol.15 (10), p.7091-7098
Main Authors: Edwards, Devin T, Faulk, Jaevyn K, Sanders, Aric W, Bull, Matthew S, Walder, Robert, LeBlanc, Marc-Andre, Sousa, Marcelo C, Perkins, Thomas T
Format: Article
Language:English
Subjects:
Atomic force microscopy
Cantilever beams
Folding
Letter
Masking
Microscopy, Atomic Force - methods
Nanostructure
Proteins
Spectroscopy
Spectrum Analysis - methods
Temporal resolution
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