scholarly journals Structure and Dynamics of Membrane-embedded KcsA Potassium Channel Revealed by Atomic Force Microscopy

2015 ◽  
Vol 55 (1) ◽  
pp. 005-010 ◽  
Author(s):  
Ayumi SUMINO ◽  
Daisuke YAMAMOTO ◽  
Takashi SUMIKAMA ◽  
Masayuki IWAMOTO ◽  
Takehisa DEWA ◽  
...  
Keyword(s):  
Atomic Force Microscopy ◽  
Potassium Channel ◽  
Force Microscopy ◽  
Structure And Dynamics ◽  
Atomic Force ◽  
Kcsa Potassium Channel

Direct Visualization of KirBac3.1 Potassium Channel Gating by Atomic Force Microscopy

2007 ◽  
Vol 374 (2) ◽  
pp. 500-505 ◽  
Author(s):  
Szymon Jarosławski ◽  
Brittany Zadek ◽  
Frances Ashcroft ◽  
Catherine Vénien-Bryan ◽  
Simon Scheuring
Keyword(s):  
Atomic Force Microscopy ◽  
Potassium Channel ◽  
Channel Gating ◽  
Direct Visualization ◽  
Force Microscopy ◽  
Atomic Force ◽  
Potassium Channel Gating

scholarly journals A comparison of the network structure and inner dynamics of homogeneously and heterogeneously crosslinked PNIPAM microgels with high crosslinker content

Soft Matter ◽  
2019 ◽  
Vol 15 (5) ◽  
pp. 1053-1064 ◽  
Author(s):  
Judith Witte ◽  
Tetyana Kyrey ◽  
Jana Lutzki ◽  
Anna Margarethe Dahl ◽  
Judith Houston ◽  
...  
Keyword(s):  
Atomic Force Microscopy ◽  
Network Structure ◽  
Force Microscopy ◽  
Structure And Dynamics ◽  
Atomic Force ◽  
Crosslinker Content

The network structure and dynamics of different PNIPAM microgels is studied with various scattering methods and atomic force microscopy.

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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