Reverse Engineering of an Affinity-Switchable Molecular Interaction Characterized by Atomic Force Microscopy Single-Molecule Force Spectroscopy†

Langmuir ◽  
2008 ◽  
Vol 24 (4) ◽  
pp. 1365-1370 ◽  
Author(s):  
Dario Anselmetti ◽  
Frank Wilco Bartels ◽  
Anke Becker ◽  
Björn Decker ◽  
Rainer Eckel ◽  
...  
ACS Nano ◽  
2017 ◽  
Vol 12 (1) ◽  
pp. 198-207 ◽  
Author(s):  
Robert Walder ◽  
William J. Van Patten ◽  
Ayush Adhikari ◽  
Thomas T. Perkins

Langmuir ◽  
2000 ◽  
Vol 16 (9) ◽  
pp. 4305-4308 ◽  
Author(s):  
Wenke Zhang ◽  
Qiaobing Xu ◽  
Shan Zou ◽  
Hongbin Li ◽  
Weiqing Xu ◽  
...  

Nanomaterials ◽  
2021 ◽  
Vol 11 (9) ◽  
pp. 2424
Author(s):  
Lyan M. van der Sleen ◽  
Katarzyna M. Tych

The mechanical properties of proteins can be studied with single molecule force spectroscopy (SMFS) using optical tweezers, atomic force microscopy and magnetic tweezers. It is common to utilize a flexible linker between the protein and trapped probe to exclude short-range interactions in SMFS experiments. One of the most prevalent linkers is DNA due to its well-defined properties, although attachment strategies between the DNA linker and protein or probe may vary. We will therefore provide a general overview of the currently existing non-covalent and covalent bioconjugation strategies to site-specifically conjugate DNA-linkers to the protein of interest. In the search for a standardized conjugation strategy, considerations include their mechanical properties in the context of SMFS, feasibility of site-directed labeling, labeling efficiency, and costs.


2015 ◽  
Vol 44 (11) ◽  
pp. 3617-3638 ◽  
Author(s):  
Yuping Shan ◽  
Hongda Wang

The structure and function of cell membranes were revealed by atomic force microscopy and force spectroscopy at the molecule level.


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