scholarly journals Real Time Single Molecular Imaging of Enzymatic Degradation of Crystalline Cellulose by High-speed Atomic Force Microscopy

2013 ◽  
Vol 53 (3) ◽  
pp. 140-144
Author(s):  
Kiyohiko IGARASHI ◽  
Takayuki UCHIHASHI ◽  
Masahiro SAMEJIMA ◽  
Toshio ANDO
Keyword(s):  
Atomic Force Microscopy ◽  
Molecular Imaging ◽  
Real Time ◽  
High Speed ◽  
Enzymatic Degradation ◽  
Crystalline Cellulose ◽  
Force Microscopy ◽  
Atomic Force

Real-time observation of solubilization-induced morphological change in surfactant aggregates adsorbed on a solid surface

2017 ◽  
Vol 53 (98) ◽  
pp. 13172-13175 ◽  
Author(s):  
Keito Koizumi ◽  
Masaaki Akamatsu ◽  
Kenichi Sakai ◽  
Shinya Sasaki ◽  
Hideki Sakai
Keyword(s):  
Atomic Force Microscopy ◽  
Real Time ◽  
Morphological Change ◽  
Solid Surface ◽  
High Speed ◽  
Force Microscopy ◽  
Surfactant Aggregates ◽  
Atomic Force ◽  
Time Observation ◽  
Real Time Observation

A solubilization-induced morphological change in surfactant surface aggregates was imaged in real-time, using high-speed atomic force microscopy.

scholarly journals High Speed Atomic Force Microscopy Visualizes Processive Movement ofTrichoderma reeseiCellobiohydrolase I on Crystalline Cellulose

2009 ◽  
Vol 284 (52) ◽  
pp. 36186-36190 ◽  
Author(s):  
Kiyohiko Igarashi ◽  
Anu Koivula ◽  
Masahisa Wada ◽  
Satoshi Kimura ◽  
Merja Penttilä ◽  
...  
Keyword(s):  
Atomic Force Microscopy ◽  
High Speed ◽  
Crystalline Cellulose ◽  
Force Microscopy ◽  
Atomic Force

scholarly journals Real-space and real-time dynamics of CRISPR-Cas9 visualized by high-speed atomic force microscopy

2017 ◽  
Vol 8 (1) ◽  
Author(s):  
Mikihiro Shibata ◽  
Hiroshi Nishimasu ◽  
Noriyuki Kodera ◽  
Seiichi Hirano ◽  
Toshio Ando ◽  
...  
Keyword(s):  
Atomic Force Microscopy ◽  
Real Time ◽  
High Speed ◽  
Real Space ◽  
Time Dynamics ◽  
Force Microscopy ◽  
Atomic Force

scholarly journals Real-Time Observation of Enzymatic Polyhydroxyalkanoate Polymerization Using High-Speed Scanning Atomic Force Microscopy

ACS Omega ◽  
2017 ◽  
Vol 2 (1) ◽  
pp. 181-185 ◽  
Author(s):  
Kazunori Ushimaru ◽  
Shoji Mizuno ◽  
Ayako Honya ◽  
Hideki Abe ◽  
Takeharu Tsuge
Keyword(s):  
Atomic Force Microscopy ◽  
Real Time ◽  
High Speed ◽  
Force Microscopy ◽  
Atomic Force ◽  
Time Observation ◽  
Real Time Observation

scholarly journals High-Speed Atomic Force Microscopy Reveals the Structural Dynamics of the Amyloid-β and Amylin Aggregation Pathways

2020 ◽  
Vol 21 (12) ◽  
pp. 4287
Author(s):  
Takahiro Watanabe-Nakayama ◽  
Bikash R. Sahoo ◽  
Ayyalusamy Ramamoorthy ◽  
Kenjiro Ono
Keyword(s):  
Atomic Force Microscopy ◽  
Protein Structure ◽  
Real Time ◽  
Structural Dynamics ◽  
High Speed ◽  
Amyloid Β ◽  
Force Microscopy ◽  
Structure And Dynamics ◽  
Atomic Force ◽  
Novel Therapeutic Strategies

Individual Alzheimer’s disease (AD) patients have been shown to have structurally distinct amyloid-β (Aβ) aggregates, including fibrils, in their brain. These findings suggest the possibility of a relationship between AD progression and Aβ fibril structures. Thus, the characterization of the structural dynamics of Aβ could aid the development of novel therapeutic strategies and diagnosis. Protein structure and dynamics have typically been studied separately. Most of the commonly used biophysical approaches are limited in providing substantial details regarding the combination of both structure and dynamics. On the other hand, high-speed atomic force microscopy (HS-AFM), which simultaneously visualizes an individual protein structure and its dynamics in liquid in real time, can uniquely link the structure and the kinetic details, and it can also unveil novel insights. Although amyloidogenic proteins generate heterogeneously aggregated species, including transient unstable states during the aggregation process, HS-AFM elucidated the structural dynamics of individual aggregates in real time in liquid without purification and isolation. Here, we review and discuss the HS-AFM imaging of amyloid aggregation and strategies to optimize the experiments showing findings from Aβ and amylin, which is associated with type II diabetes, shares some common biological features with Aβ, and is reported to be involved in AD.

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