Single-molecule determination of chemical equilibrium of DNA intercalation by electrical conductance

2021 ◽  
Author(s):  
Lu Zhang ◽  
Satoshi Kaneko ◽  
Shintaro Fujii ◽  
Manabu Kiguchi ◽  
Tomoaki Nishino

We investigated a single-molecule reaction of DNA intercalation as an example of a bimolecular association reaction. Single-molecule conductance values of the product and reactant molecules adsorbed on an Au surface...


Author(s):  
Pablo Luis Hernández-Adame ◽  
Ulises Meza ◽  
Aldo A. Rodríguez-Menchaca ◽  
Sergio Sánchez-Armass ◽  
Jaime Ruiz-García ◽  
...  


2000 ◽  
Vol 355 (1396) ◽  
pp. 441-447 ◽  
Author(s):  
T. Yanagida ◽  
S. Esaki ◽  
A. Hikikoshi Iwane ◽  
Y. Inoue ◽  
A. Ishijima ◽  
...  

Recent progress in single–molecule detection techniques is remarkable. These techniques have allowed the accurate determination of myosin–head–induced displacements and how mechanical cycles are coupled to ATP hydrolysis, by measuring individual mechanical events and chemical events of actomyosin directly at the single–molecule level. Here we review our recent work in which we have made detailed measurements of myosin step size and mechanochemical coupling, and propose a model of the myosin motor.





2008 ◽  
Vol 108 (10) ◽  
pp. 1135-1139 ◽  
Author(s):  
Mélanie Favre ◽  
Serguei K. Sekatskii ◽  
Giovanni Dietler


1968 ◽  
Vol 72 (12) ◽  
pp. 4314-4316 ◽  
Author(s):  
Vaidyanathaiyer Subrahmanyan ◽  
N. Lakshminarayanaiah


2020 ◽  
Author(s):  
Mike Filius ◽  
Sung Hyun Kim ◽  
Ivo Severins ◽  
Chirlmin Joo

ABSTRACTSingle-molecule FRET is a versatile tool to study nucleic acids and proteins at the nanometer scale. However, currently, only a couple of FRET pairs can be reliably measured on a single object. The limited number of available FRET pair fluorophores and complicated data analysis makes it challenging to apply single-molecule FRET for structural analysis of biomolecules. Currently, only a couple of FRET pairs can be reliably measured on a single object. Here we present an approach that allows for the determination of multiple distances between FRET pairs in a single object. We use programmable, transient binding between short DNA strands to resolve the FRET efficiency of multiple fluorophore pairs. By allowing only a single FRET pair to be formed at a time, we can determine the FRET efficiency and pair distance with sub-nanometer resolution. We determine the distance between other pairs by sequentially exchanging DNA strands. We name this multiplexing approach FRET X for FRET via DNA eXchange. We envision that our FRET X technology will be a tool for the high-resolution structural analysis of biomolecules and other nano-structures.



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