Ultrafast structural dynamics in electronically excited solid neon. I. Real-time probing of the electronic bubble formation

2003 ◽  
Vol 67 (11) ◽  
Author(s):  
Franco Vigliotti ◽  
Luigi Bonacina ◽  
Majed Chergui
2016 ◽  
Vol 7 (1) ◽  
pp. 619-627 ◽  
Author(s):  
Xinxin Cheng ◽  
Yan Gao ◽  
Fedor Rudakov ◽  
Peter M. Weber

Time-resolved Rydberg fingerprint spectroscopy combined with quantum chemical calculations reveals the complex structural dynamics and charge transfer in real time.


2011 ◽  
Vol 96 (10) ◽  
pp. 1788-1792 ◽  
Author(s):  
J.B.A. Mitchell ◽  
E. Jerby ◽  
Y. Shamir ◽  
Y. Meir ◽  
J.L. Le Garrec ◽  
...  

2020 ◽  
Vol 21 (12) ◽  
pp. 4287
Author(s):  
Takahiro Watanabe-Nakayama ◽  
Bikash R. Sahoo ◽  
Ayyalusamy Ramamoorthy ◽  
Kenjiro Ono

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.


Author(s):  
S.J. Wang ◽  
T. Dyakowski ◽  
C.G. Xie ◽  
R.A. Williams ◽  
M.S. Beck

1991 ◽  
Vol 237 ◽  
Author(s):  
Walter P. Lowe ◽  
Roy Clarke

ABSTRACTWe present dynamic structural studies of thin films and their interface with underlying substrates using real-time x-ray diffraction. Using synchrotron light we have observed, in real-time, interface dynamics in semiconductor systems such as GexSi(i−x)/Si. The measurements show that under large temperature changes thin epitaxial layers may behave cooperatively to modify the overall strain profile. Dynamic behavior is exhibited in a series of discontinuities in the perpendicular lattice constant of the overlayer.


2008 ◽  
Vol 95 (1) ◽  
pp. 233-239 ◽  
Author(s):  
Stefan Kowarik ◽  
Alexander Gerlach ◽  
Stefan Sellner ◽  
Leide Cavalcanti ◽  
Oleg Konovalov ◽  
...  

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