Fast imaging method combining cantilever and feedback signals in contact-mode atomic force microscopy

1999 ◽  
Vol 69 (1) ◽  
pp. 51-54 ◽  
Author(s):  
S. Yumoto ◽  
N. Ookubo
Keyword(s):  
Atomic Force Microscopy ◽  
Fast Imaging ◽  
Imaging Method ◽  
Contact Mode ◽  
Force Microscopy ◽  
Atomic Force ◽  
Mode Atomic Force Microscopy

Vibrational Response of FeNi3Nanoparticles to the Flux of a Modulated Electromagnetic Field Detected by Contact-Mode Atomic Force Microscopy

2013 ◽  
Vol 117 (36) ◽  
pp. 18768-18776 ◽  
Author(s):  
Algernon T. Kelley ◽  
Wilson K. Serem ◽  
Stephanie L. Daniels ◽  
Lauren E. Englade-Franklin ◽  
Gregory Morrison ◽  
...  
Keyword(s):  
Atomic Force Microscopy ◽  
Electromagnetic Field ◽  
Contact Mode ◽  
Force Microscopy ◽  
Vibrational Response ◽  
Atomic Force ◽  
Mode Atomic Force Microscopy

scholarly journals Structural Evidence for α-Synuclein Fibrils Using in Situ Atomic Force Microscopy

2005 ◽  
Vol 37 (2) ◽  
pp. 113-118
Author(s):  
Feng Zhang ◽  
Li-Na Ji ◽  
Lin Tang ◽  
Jun Hu ◽  
Hong-Yu Hu ◽  
...  
Keyword(s):  
Atomic Force Microscopy ◽  
Guanidine Hydrochloride ◽  
Indirect Evidence ◽  
Contact Mode ◽  
Microscopy Imaging ◽  
Tapping Mode ◽  
Force Microscopy ◽  
Atomic Force ◽  
Mode Atomic Force Microscopy

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.

Contact mode atomic force microscopy imaging of nanometer‐sized particles

1995 ◽  
Vol 66 (24) ◽  
pp. 3295-3297 ◽  
Author(s):  
T. Junno ◽  
S. Anand ◽  
K. Deppert ◽  
L. Montelius ◽  
L. Samuelson
Keyword(s):  
Atomic Force Microscopy ◽  
Contact Mode ◽  
Microscopy Imaging ◽  
Force Microscopy ◽  
Atomic Force ◽  
Atomic Force Microscopy Imaging ◽  
Mode Atomic Force Microscopy
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