Mechanical properties of cardiac titin’s N2B-region by single-molecule atomic force spectroscopy

2006 ◽  
Vol 155 (2) ◽  
pp. 263-272 ◽  
Author(s):  
Mark C. Leake ◽  
Anika Grützner ◽  
Martina Krüger ◽  
Wolfgang A. Linke
Keyword(s):  
Mechanical Properties ◽  
Single Molecule ◽  
Force Spectroscopy ◽  
Atomic Force Spectroscopy ◽  
Atomic Force

scholarly journals Investigating Single Molecule Adhesion by Atomic Force Spectroscopy

10.3791/52456 ◽  
2015 ◽  
Author(s):  
Frank W. S. Stetter ◽  
Sandra Kienle ◽  
Stefanie Krysiak ◽  
Thorsten Hugel
Keyword(s):  
Single Molecule ◽  
Force Spectroscopy ◽  
Atomic Force Spectroscopy ◽  
Atomic Force

scholarly journals Denaturation transition of stretched DNA

2013 ◽  
Vol 41 (2) ◽  
pp. 639-645 ◽  
Author(s):  
Andreas Hanke
Keyword(s):  
Nucleic Acids ◽  
Single Molecule ◽  
Force Spectroscopy ◽  
Magnetic Tweezers ◽  
Present Review ◽  
Dna Molecules ◽  
Force Measurements ◽  
Force Extension ◽  
Atomic Force Spectroscopy ◽  
Atomic Force

In the last two decades, single-molecule force measurements using optical and magnetic tweezers and atomic force spectroscopy have dramatically expanded our knowledge of nucleic acids and proteins. These techniques characterize the force on a biomolecule required to produce a given molecular extension. When stretching long DNA molecules, the observed force–extension relationship exhibits a characteristic plateau at approximately 65 pN where the DNA may be extended to almost twice its B-DNA length with almost no increase in force. In the present review, I describe this transition in terms of the Poland–Scheraga model and summarize recent related studies.

scholarly journals Single-Molecule Atomic-Force Spectroscopy Captures a Novel Class of Molecular Nanosprings with Robust Stepwise Refolding Properties

2010 ◽  
Vol 98 (3) ◽  
pp. 593a-594a
Author(s):  
Minkyu Kim ◽  
Khadar Abdi ◽  
Gwangrog Lee ◽  
Mahir Rabbi ◽  
Whasil Lee ◽  
...  
Keyword(s):  
Single Molecule ◽  
Force Spectroscopy ◽  
Atomic Force Spectroscopy ◽  
Atomic Force

Testing synthetic amyloid-β aggregation inhibitor using single molecule atomic force spectroscopy

2014 ◽  
Vol 54 ◽  
pp. 492-498 ◽  
Author(s):  
Francis T. Hane ◽  
Brenda Y. Lee ◽  
Anahit Petoyan ◽  
Arvi Rauk ◽  
Zoya Leonenko
Keyword(s):  
Single Molecule ◽  
Amyloid Β ◽  
Force Spectroscopy ◽  
Atomic Force Spectroscopy ◽  
Atomic Force ◽  
Aggregation Inhibitor

scholarly journals Bioconjugation Strategies for Connecting Proteins to DNA-Linkers for Single-Molecule Force-Based Experiments

Nanomaterials ◽  
2021 ◽  
Vol 11 (9) ◽  
pp. 2424
Author(s):  
Lyan M. van der Sleen ◽  
Katarzyna M. Tych
Keyword(s):  
Mechanical Properties ◽  
Atomic Force Microscopy ◽  
Optical Tweezers ◽  
Single Molecule ◽  
Short Range ◽  
Force Spectroscopy ◽  
Magnetic Tweezers ◽  
Single Molecule Force Spectroscopy ◽  
Force Microscopy ◽  
Atomic Force

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.

scholarly journals Concurrent Atomic Force Spectroscopy

2018 ◽  
Author(s):  
Carolina Pimenta-Lopes ◽  
Carmen Suay-Corredera ◽  
Diana Velázquez-Carreras ◽  
David Sánchez-Ortiz ◽  
Jorge Alegre-Cebollada
Keyword(s):  
Mechanical Properties ◽  
Atomic Force Microscopy ◽  
Single Molecule ◽  
Mechanical Characterization ◽  
Force Spectroscopy ◽  
Fold Increase ◽  
Force Measurements ◽  
Force Microscopy ◽  
Atomic Force ◽  
Calibration Uncertainty

ABSTRACTForce-spectroscopy by Atomic Force Microscopy (AFM) is the technique of choice to measure mechanical properties of molecules, cells, tissues and materials at the nano and micro scales. However, unavoidable calibration errors of AFM probes make it cumbersome to quantify modulation of mechanics. Here, we show that concurrent AFM force measurements enable relative mechanical characterization with an accuracy that is independent of calibration uncertainty, even when averaging data from multiple, independent experiments. Compared to traditional AFM, we estimate that concurrent strategies can measure differences in protein mechanical unfolding forces with a 6-fold improvement in accuracy and a 30-fold increase in throughput. Prompted by our results, we demonstrate widely applicable orthogonal fingerprinting strategies for concurrent single-molecule nanomechanical profiling of proteins.

scholarly journals Single-Molecule Atomic Force Spectroscopy Reveals that DnaD Forms Scaffolds and Enhances Duplex Melting

2008 ◽  
Vol 377 (3) ◽  
pp. 706-714 ◽  
Author(s):  
Wenke Zhang ◽  
Cristina Machón ◽  
Alberto Orta ◽  
Nicola Phillips ◽  
Clive J. Roberts ◽  
...  
Keyword(s):  
Single Molecule ◽  
Force Spectroscopy ◽  
Atomic Force Spectroscopy ◽  
Atomic Force
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