Phase, Structure, and Dynamics of the Hydration Layer Probed by Atomic Force Microscopy

2019 ◽  
Vol 123 (35) ◽  
pp. 21528-21537 ◽  
Author(s):  
Liyi Bai ◽  
Zhengqing Zhang ◽  
Joonkyung Jang
Keyword(s):  
Atomic Force Microscopy ◽  
Phase Structure ◽  
Hydration Layer ◽  
Force Microscopy ◽  
Structure And Dynamics ◽  
Atomic Force

scholarly journals Three-dimensional hydration layer mapping on the (10.4) surface of calcite using amplitude modulation atomic force microscopy

2014 ◽  
Vol 25 (33) ◽  
pp. 335703 ◽  
Author(s):  
Christoph Marutschke ◽  
Deron Walters ◽  
Jason Cleveland ◽  
Ilka Hermes ◽  
Ralf Bechstein ◽  
...  
Keyword(s):  
Atomic Force Microscopy ◽  
Amplitude Modulation ◽  
Three Dimensional ◽  
Hydration Layer ◽  
Force Microscopy ◽  
Atomic Force

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

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.

scholarly journals Pulse-response measurement of frequency-resolved water dynamics on a hydrophilic surface using a Q-damped atomic force microscopy cantilever

2012 ◽  
Vol 3 ◽  
pp. 260-266
Author(s):  
Masami Kageshima
Keyword(s):  
Atomic Force Microscopy ◽  
Pulse Response ◽  
Water Dynamics ◽  
Control Technique ◽  
Response Measurement ◽  
Hydration Layer ◽  
Force Microscopy ◽  
Resonance Modes ◽  
Atomic Force ◽  
Atomic Force Microscopy Cantilever

The frequency-resolved viscoelasticity of a hydration layer on a mica surface was studied by pulse-response measurement of a magnetically driven atomic force microscopy cantilever. Resonant ringing of the cantilever due to its 1st and 2nd resonance modes was suppressed by means of the Q-control technique. The Fourier–Laplace transform of the deflection signal of the cantilever gave the frequency-resolved complex compliance of the cantilever–sample system. The significant viscoelasticity spectrum of the hydration layer was successfully derived in a frequency range below 100 kHz by comparison of data obtained at a distance of 300 nm from the substrate with those taken in the proximity of the substrate. A positive value of the real part of the stiffness was determined and is attributed to the reported solidification of the hydration layers.

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