scholarly journals Blue light-induced low mechanical stability of ruthenium-based coordination bonds: an AFM-based single-molecule force spectroscopy study

RSC Advances ◽  
2020 ◽  
Vol 10 (66) ◽  
pp. 40543-40551
Author(s):  
Mohd. Muddassir
Keyword(s):  
Blue Light ◽  
Single Molecule ◽  
Mechanical Stability ◽  
Force Spectroscopy ◽  
Spectroscopy Study ◽  
Force Extension ◽  
Single Molecule Force Spectroscopy ◽  
Amide Bonds ◽  
Coordination Bonds

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.

scholarly journals Single molecule force spectroscopy studies of DNA denaturation by T4 gene 32 protein

2004 ◽  
Vol 18 (2) ◽  
pp. 203-211 ◽  
Author(s):  
Mark C. Williams ◽  
Kiran Pant ◽  
Ioulia Rouzina ◽  
Richard L. Karpel
Keyword(s):  
Dna Binding ◽  
Optical Tweezers ◽  
Single Molecule ◽  
Protein Interactions ◽  
Force Spectroscopy ◽  
Melting Transition ◽  
Dna Molecules ◽  
Force Extension ◽  
Single Molecule Force Spectroscopy ◽  
Gene 32

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.

scholarly journals Single-Molecule Force Spectroscopy Study on Modular Resilin Fusion Protein

ACS Omega ◽  
2017 ◽  
Vol 2 (10) ◽  
pp. 6906-6915 ◽  
Author(s):  
Alessandra Griffo ◽  
Hendrik Hähl ◽  
Samuel Grandthyll ◽  
Frank Müller ◽  
Arja Paananen ◽  
...  
Keyword(s):  
Fusion Protein ◽  
Single Molecule ◽  
Force Spectroscopy ◽  
Spectroscopy Study ◽  
Single Molecule Force Spectroscopy

Single molecule force spectroscopy reveals that the oxidation state of cobalt ions plays an important role in enhancing the mechanical stability of proteins

Nanoscale ◽  
2019 ◽  
Vol 11 (42) ◽  
pp. 19791-19796 ◽  
Author(s):  
Jiahao Xia ◽  
Jiacheng Zuo ◽  
Hongbin Li
Keyword(s):  
Oxidation State ◽  
Single Molecule ◽  
Mechanical Stability ◽  
Force Spectroscopy ◽  
Metal Chelation ◽  
Single Molecule Force Spectroscopy ◽  
Cobalt Ions

The binding of Co(iii) to the bi-histidine metal chelation site significantly enhances protein's mechanical stability.

scholarly journals Single-Molecule Force Spectroscopy Study on the Mechanism of RNA Disassembly in Tobacco Mosaic Virus

2013 ◽  
Vol 105 (12) ◽  
pp. 2790-2800 ◽  
Author(s):  
Ningning Liu ◽  
Ying Chen ◽  
Bo Peng ◽  
Yuan Lin ◽  
Qian Wang ◽  
...  
Keyword(s):  
Tobacco Mosaic Virus ◽  
Mosaic Virus ◽  
Single Molecule ◽  
Force Spectroscopy ◽  
Spectroscopy Study ◽  
Single Molecule Force Spectroscopy

scholarly journals Molecular mechanism of extreme mechanostability in a pathogen adhesin

Science ◽  
2018 ◽  
Vol 359 (6383) ◽  
pp. 1527-1533 ◽  
Author(s):  
Lukas F. Milles ◽  
Klaus Schulten ◽  
Hermann E. Gaub ◽  
Rafael C. Bernardi
Keyword(s):  
Single Molecule ◽  
Mechanical Stability ◽  
Force Spectroscopy ◽  
Covalent Bond ◽  
Binding Pocket ◽  
Peptide Backbone ◽  
Human Fibrinogen ◽  
Single Molecule Force Spectroscopy ◽  
Force Microscopy ◽  
Dynamics Simulations

High resilience to mechanical stress is key when pathogens adhere to their target and initiate infection. Using atomic force microscopy–based single-molecule force spectroscopy, we explored the mechanical stability of the prototypical staphylococcal adhesin SdrG, which targets a short peptide from human fibrinogen β. Steered molecular dynamics simulations revealed, and single-molecule force spectroscopy experiments confirmed, the mechanism by which this complex withstands forces of over 2 nanonewtons, a regime previously associated with the strength of a covalent bond. The target peptide, confined in a screwlike manner in the binding pocket of SdrG, distributes forces mainly toward the peptide backbone through an intricate hydrogen bond network. Thus, these adhesins can attach to their target with exceptionally resilient mechanostability, virtually independent of peptide side chains.

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