Evaluation of elastic modulus of ultra-thin vermiculite membranes by contact mode atomic force microscopy imaging

2013 ◽  
Vol 527 ◽  
pp. 205-209 ◽  
Author(s):  
Ji Won Suk ◽  
Richard D. Piner ◽  
Jinho An ◽  
Rodney S. Ruoff
1995 ◽  
Vol 66 (24) ◽  
pp. 3295-3297 ◽  
Author(s):  
T. Junno ◽  
S. Anand ◽  
K. Deppert ◽  
L. Montelius ◽  
L. Samuelson

2017 ◽  
Vol 8 ◽  
pp. 1563-1570 ◽  
Author(s):  
Juan Ren ◽  
Qingze Zou

Adaptive multiloop-mode (AMLM) imaging to substantially increase (over an order of magnitude) the speed of tapping-mode (TM) imaging is tested and evaluated through imaging three largely different heterogeneous polymer samples in experiments. It has been demonstrated that AMLM imaging, through the combination of a suite of advanced control techniques, is promising to achieve high-speed dynamic-mode atomic force microscopy imaging. The performance, usability, and robustness of the AMLM in various imaging applications, however, is yet to be assessed. In this work, three benchmark polymer samples, including a PS–LDPE sample, an SBS sample, and a Celgard sample, differing in feature size and stiffness of two orders of magnitude, are imaged using the AMLM technique at high-speeds of 25 Hz and 20 Hz, respectively. The comparison of the images obtained to those obtained by using TM imaging at scan rates of 1 Hz and 2 Hz showed that the quality of the 25 Hz and 20 Hz AMLM imaging is at the same level of that of the 1 Hz TM imaging, while the tip–sample interaction force is substantially smaller than that of the 2 Hz TM imaging.


2005 ◽  
Vol 37 (2) ◽  
pp. 113-118
Author(s):  
Feng Zhang ◽  
Li-Na Ji ◽  
Lin Tang ◽  
Jun Hu ◽  
Hong-Yu Hu ◽  
...  

Abstract Human α-synuclein is a presynaptic terminal protein and can form insoluble fibrils that are believed to play an important role in the pathogenesis of several neurodegenerative diseases such as Parkinson's disease, dementia with Lewy bodies and Lewy body variant of Alzheimer's disease. In this paper, in situ atomic force microscopy has been used to study the structural properties of α-synuclein fibrils in solution using two different atomic force microscopy imaging modes: tapping mode and contact mode. In the in situ contact mode atomic force microscopy experiments α-synuclein fibrils quickly broke into fragments, and a similar phenomenon was found using tapping mode atomic force microscopy in which α-synuclein fibrils were incubated with guanidine hydrochloride (0.6 M). The α-synuclein fibrils kept their original filamentous topography for over 1 h in the in situ tapping mode atomic force microscopy experiments. The present results provide indirect evidence on how β-sheets assemble into α-synuclein fibrils on a nanometer scale.


Nano Research ◽  
2012 ◽  
Vol 5 (4) ◽  
pp. 235-247 ◽  
Author(s):  
Rouholla Alizadegan ◽  
Albert D. Liao ◽  
Feng Xiong ◽  
Eric Pop ◽  
K. Jimmy Hsia

2013 ◽  
Vol 56 (9) ◽  
pp. 811-817 ◽  
Author(s):  
Mi Li ◽  
LianQing Liu ◽  
Ning Xi ◽  
YueChao Wang ◽  
ZaiLi Dong ◽  
...  

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