scholarly journals Rate-dependent force–extension models for single-molecule force spectroscopy experiments

2020 ◽  
Vol 17 (5) ◽  
pp. 056002 ◽  
Author(s):  
Manon Benedito ◽  
Fabio Manca ◽  
Pier Luca Palla ◽  
Stefano Giordano
2004 ◽  
Vol 18 (2) ◽  
pp. 203-211 ◽  
Author(s):  
Mark C. Williams ◽  
Kiran Pant ◽  
Ioulia Rouzina ◽  
Richard L. Karpel

Single molecule force spectroscopy is an emerging technique that can be used to measure the biophysical properties of single macromolecules such as nucleic acids and proteins. In particular, single DNA molecule stretching experiments are used to measure the elastic properties of these molecules and to induce structural transitions. We have demonstrated that double‒stranded DNA molecules undergo a force‒induced melting transition at high forces. Force–extension measurements of single DNA molecules using optical tweezers allow us to measure the stability of DNA under a variety of solution conditions and in the presence of DNA binding proteins. Here we review the evidence of DNA melting in these experiments and discuss the example of DNA force‒induced melting in the presence of the single‒stranded DNA binding protein T4 gene 32. We show that this force spectroscopy technique is a useful probe of DNA–protein interactions, which allows us to obtain binding rates and binding free energies for these interactions.


Author(s):  
Chandrayee Mukherjee ◽  
Manindra Bera ◽  
Sri Rama Koti Ainavarapu ◽  
Kaushik Sengupta

The fundamental unit of the human body comprises of the cells which remain embedded in a fibrillar network of extracellular matrix proteins which in turn provides necessary anchorage the cells. Tissue repair, regeneration and reprogramming predominantly involve a traction force mediated signalling originating in the ECM and travelling deep into the cell including the nucleus via circuitry of spring-like filamentous proteins like microfilaments or actin, intermediate filaments and microtubules to elicit a response in the form of mechanical movement as well as biochemical changes. The ‘springiness’ of these proteins is highlighted in their extension–contraction behaviour which is manifested as an effect of differential traction force. Atomic force microscope (AFM) provides the magic eye to visualize and quantify such force-extension/indentation events in these filamentous proteins as well as in whole cells. In this review, we have presented a summary of the current understanding and advancement of such measurements by AFM based single-molecule force spectroscopy in the context of cytoskeletal and nucleoskeletal proteins which act in tandem to facilitate mechanotransduction.


RSC Advances ◽  
2020 ◽  
Vol 10 (66) ◽  
pp. 40543-40551
Author(s):  
Mohd. Muddassir

A HA–RuII complex was conjugated to a hyaluronan polymer through amide bonds. In AFM experiments using the “multi-fishhook” approach, the cantilever tip made contact with the polymeric molecule, resulting in stretching, indicated by sawtooth-like force-extension curves.


2021 ◽  
Vol 714 (3) ◽  
pp. 032023
Author(s):  
Ling Chen ◽  
Liya Yang ◽  
Chunxia Wang ◽  
Ting Zhu

2010 ◽  
Vol 132 (32) ◽  
pp. 11036-11038 ◽  
Author(s):  
Ningning Liu ◽  
Bo Peng ◽  
Yuan Lin ◽  
Zhaohui Su ◽  
Zhongwei Niu ◽  
...  

Langmuir ◽  
2010 ◽  
Vol 26 (12) ◽  
pp. 9491-9496 ◽  
Author(s):  
Ningning Liu ◽  
Tianjia Bu ◽  
Yu Song ◽  
Wei Zhang ◽  
Jinjing Li ◽  
...  

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