The Hyphenated Technique of High Speed Atomic Force Microscopy and Super Resolution Optical Detection System

2018 ◽  
pp. 105-130
Author(s):  
Xiao Feng ◽  
Yunchang Guo ◽  
Hongjie An ◽  
Hongshun Yang
Keyword(s):  
Atomic Force Microscopy ◽  
High Speed ◽  
Detection System ◽  
Optical Detection ◽  
Super Resolution ◽  
Force Microscopy ◽  
Hyphenated Technique ◽  
Atomic Force ◽  
Optical Detection System

A high-speed atomic force microscopy with super resolution based on path planning scanning

2020 ◽  
Vol 213 ◽  
pp. 112991
Author(s):  
Yinan Wu ◽  
Yongchun Fang ◽  
Chao Wang ◽  
Cunhuan Liu ◽  
Zhi Fan
Keyword(s):  
Atomic Force Microscopy ◽  
Path Planning ◽  
High Speed ◽  
Super Resolution ◽  
Force Microscopy ◽  
Atomic Force

Amplitude Estimation Technique for Intermittent Contact Atomic Force Microscopy

2017 ◽  
Vol 6 (2) ◽  
pp. 29-42
Author(s):  
Grzegorz Dobiński ◽  
Sławomir Pawłowski ◽  
Marek Smolny
Keyword(s):  
Atomic Force Microscopy ◽  
High Speed ◽  
Detection System ◽  
Measurement Techniques ◽  
Estimation Method ◽  
High Speed Imaging ◽  
Force Microscopy ◽  
Atomic Force ◽  
Amplitude Estimation ◽  
Intermittent Contact

This article describes how one of the biggest challenges in designing of high-speed intermittent contact atomic force microscope (AFM) is the construction of a fast amplitude detector. The measurement techniques commonly used in commercial microscopes, such as RMS to DC converters or lock-in amplifiers often do not provide sufficient bandwidth to perform high speed imaging. On the other hand, many techniques developed especially for high-speed AFM are characterized by poor signal-to-noise ratio. In this paper, a novel amplitude estimation method based on the generalized Goertzel algorithm is presented. The detection system, composed of 16-bit 100 mega-samples per second analog-to-digital converter and field-programmable gate array device, allows to measure the signal amplitude within the time comparable to one oscillation cycle of the AFM cantilever. The effectiveness and validity of the designed detector were investigated by computer simulation. High spatial resolution of the presented method implemented in the actual atomic force microscopy system is also demonstrated.

scholarly journals Histone variant H2A.B-H2B dimers are spontaneously exchanged with canonical H2A-H2B in the nucleosome

2021 ◽  
Vol 4 (1) ◽  
Author(s):  
Rina Hirano ◽  
Yasuhiro Arimura ◽  
Tomoya Kujirai ◽  
Mikihiro Shibata ◽  
Aya Okuda ◽  
...  
Keyword(s):  
Atomic Force Microscopy ◽  
Dna Repair ◽  
High Speed ◽  
Histone Chaperones ◽  
Histone H2a ◽  
Force Microscopy ◽  
Atomic Force ◽  
Open Conformation ◽  
Replication Sites ◽  
Histone Exchange

AbstractH2A.B is an evolutionarily distant histone H2A variant that accumulates on DNA repair sites, DNA replication sites, and actively transcribing regions in genomes. In cells, H2A.B exchanges rapidly in chromatin, but the mechanism has remained enigmatic. In the present study, we found that the H2A.B-H2B dimer incorporated within the nucleosome exchanges with the canonical H2A-H2B dimer without assistance from additional factors, such as histone chaperones and nucleosome remodelers. High-speed atomic force microscopy revealed that the H2A.B nucleosome, but not the canonical H2A nucleosome, transiently forms an intermediate “open conformation”, in which two H2A.B-H2B dimers may be detached from the H3-H4 tetramer and bind to the DNA regions near the entry/exit sites. Mutational analyses revealed that the H2A.B C-terminal region is responsible for the adoption of the open conformation and the H2A.B-H2B exchange in the nucleosome. These findings provide mechanistic insights into the histone exchange of the H2A.B nucleosome.

High-Speed Atomic Force Microscopy for Studying the Dynamic Behavior of Protein Molecules at Work

2006 ◽  
Vol 45 (3B) ◽  
pp. 1897-1903 ◽  
Author(s):  
Toshio Ando ◽  
Takayuki Uchihashi ◽  
Noriyuki Kodera ◽  
Atsushi Miyagi ◽  
Ryo Nakakita ◽  
...  
Keyword(s):  
Atomic Force Microscopy ◽  
Dynamic Behavior ◽  
High Speed ◽  
Force Microscopy ◽  
Atomic Force ◽  
Protein Molecules
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