scholarly journals Single molecule force spectroscopy studies of DNA binding and chaperone proteins

2008 ◽  
Author(s):  
Fei Wang
Keyword(s):  
Dna Binding ◽  
Single Molecule ◽  
Force Spectroscopy ◽  
Chaperone Proteins ◽  
Single Molecule Force Spectroscopy ◽  
Spectroscopy Studies

Peptide Desorption Kinetics from Single Molecule Force Spectroscopy Studies

2014 ◽  
Vol 136 (2) ◽  
pp. 688-697 ◽  
Author(s):  
Stefanie Krysiak ◽  
Susanne Liese ◽  
Roland R. Netz ◽  
Thorsten Hugel
Keyword(s):  
Single Molecule ◽  
Force Spectroscopy ◽  
Desorption Kinetics ◽  
Single Molecule Force Spectroscopy ◽  
Spectroscopy Studies

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.

Membrane-based actuation for high-speed single molecule force spectroscopy studies using AFM

2010 ◽  
Vol 39 (8) ◽  
pp. 1219-1227 ◽  
Author(s):  
Krishna Sarangapani ◽  
Hamdi Torun ◽  
Ofer Finkler ◽  
Cheng Zhu ◽  
Levent Degertekin
Keyword(s):  
Single Molecule ◽  
High Speed ◽  
Force Spectroscopy ◽  
Single Molecule Force Spectroscopy ◽  
Spectroscopy Studies

scholarly journals Single-Molecule Force Spectroscopy Studies on Sumo Polyproteins Reveal their Mechanical Flexibility

2013 ◽  
Vol 104 (2) ◽  
pp. 167a ◽  
Author(s):  
Hema Chandra Kotamarthi ◽  
Riddhi Sharma ◽  
Sri Rama Koti Ainavarapu
Keyword(s):  
Single Molecule ◽  
Force Spectroscopy ◽  
Single Molecule Force Spectroscopy ◽  
Spectroscopy Studies

Aligning Molecular Attachment Sites in Single Molecule Force Spectroscopy Measurements

2008 ◽  
Author(s):  
Monica Rivera ◽  
Whasil Lee ◽  
Piotr E. Marszalek ◽  
Daniel G. Cole ◽  
Robert L. Clark
Keyword(s):  
Atomic Force Microscopy ◽  
Single Molecule ◽  
Force Spectroscopy ◽  
Alignment Program ◽  
Single Molecule Force Spectroscopy ◽  
Force Microscopy ◽  
Atomic Force ◽  
Simulated Environment ◽  
Attachment Sites ◽  
Spectroscopy Studies

In atomic force microscopy (AFM) -based single molecule force spectroscopy, it is assumed that the pulling angle is negligible and that the force applied to the molecule is equivalent to the force measured by the instrument. Although this assumption may hold for flexible, compact molecules, studies have shown that it may not be appropriate for fairly rigid molecules, where measured forces can be a fraction of the actual values experienced by the molecule. Previously, we have proposed a method to align a molecule’s substrate and cantilever attachment sites and tested it in a simulated environment. Here we continue our work and test the alignment program in an experimental environment. In this paper we demonstrate that circling-induced force fluctuations are the result of stretching and relaxing a tethered molecule and we present the results of an alignment trial. Combined, these preliminary results demonstrate the feasibility of the alignment program and are a promising step towards correcting pulling geometry errors in single molecule force spectroscopy studies.

scholarly journals Single-Molecule Force Spectroscopy Studies of APOBEC3A–Single-Stranded DNA Complexes

Biochemistry ◽  
2016 ◽  
Vol 55 (22) ◽  
pp. 3102-3106 ◽  
Author(s):  
Luda S. Shlyakhtenko ◽  
Samrat Dutta ◽  
Ming Li ◽  
Reuben S. Harris ◽  
Yuri L. Lyubchenko
Keyword(s):  
Single Molecule ◽  
Force Spectroscopy ◽  
Dna Complexes ◽  
Single Molecule Force Spectroscopy ◽  
Single Stranded Dna ◽  
Spectroscopy Studies
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