Three-dimensional domain patterns in tetragonal-to-monoclinic Bi4Ti3O12 ceramics: Nonlinear analysis and piezoresponse force microscopy imaging

2020 ◽  
Vol 188 ◽  
pp. 228-240 ◽  
Author(s):  
Shaoxiong Xie ◽  
Yu Chen ◽  
Wenyuan Liu ◽  
Guozhan Xia ◽  
Boyuan Huang ◽  
...  
Keyword(s):  
Nonlinear Analysis ◽  
Three Dimensional ◽  
Piezoresponse Force Microscopy ◽  
Microscopy Imaging ◽  
Force Microscopy ◽  
Dimensional Domain ◽  
Bi4ti3o12 Ceramics

Three-dimensional ferroelectric domain imaging of epitaxial BiFeO3 thin films using angle-resolved piezoresponse force microscopy

2010 ◽  
Vol 97 (11) ◽  
pp. 112907 ◽  
Author(s):  
Moonkyu Park ◽  
Seungbum Hong ◽  
Jeffrey A. Klug ◽  
Michael J. Bedzyk ◽  
Orlando Auciello ◽  
...  
Keyword(s):  
Thin Films ◽  
Three Dimensional ◽  
Piezoresponse Force Microscopy ◽  
Ferroelectric Domain ◽  
Force Microscopy ◽  
Bifeo3 Thin Films

Three dimensional piezoresponse force microscopy polarization difference maps

2011 ◽  
Vol 109 (7) ◽  
pp. 074110 ◽  
Author(s):  
Yuanyuan Jing ◽  
John E. Blendell ◽  
Keith J. Bowman
Keyword(s):  
Three Dimensional ◽  
Piezoresponse Force Microscopy ◽  
Force Microscopy ◽  
Polarization Difference

Three-dimensional domain swapping and supramolecular protein assembly: insights from the X-ray structure of a dimeric swapped variant of human pancreatic RNase

2013 ◽  
Vol 69 (10) ◽  
pp. 2116-2123 ◽  
Author(s):  
Andrea Pica ◽  
Antonello Merlino ◽  
Alexander K. Buell ◽  
Tuomas P. J. Knowles ◽  
Elio Pizzo ◽  
...  
Keyword(s):  
Three Dimensional ◽  
Supramolecular Assembly ◽  
Domain Swapping ◽  
Crystallographic Axis ◽  
Force Microscopy ◽  
Atomic Force ◽  
Pancreatic Rnase ◽  
Quaternary Structures ◽  
New Evidence ◽  
Dimensional Domain

The deletion of five residues in the loop connecting the N-terminal helix to the core of monomeric human pancreatic ribonuclease leads to the formation of an enzymatically active domain-swapped dimer (desHP). The crystal structure of desHP reveals the generation of an intriguing fibril-like aggregate of desHP molecules that extends along theccrystallographic axis. Dimers are formed by three-dimensional domain swapping. Tetramers are formed by the aggregation of swapped dimers with slightly different quaternary structures. The tetramers interact in such a way as to form an infinite rod-like structure that propagates throughout the crystal. The observed supramolecular assembly captured in the crystal predicts that desHP fibrils could form in solution; this has been confirmed by atomic force microscopy. These results provide new evidence that three-dimensional domain swapping can be a mechanism for the formation of elaborate large assemblies in which the protein, apart from the swapping, retains its original fold.

scholarly journals Decoupling indirect topographic cross-talk in band excitation piezoresponse force microscopy imaging and spectroscopy

2016 ◽  
Vol 108 (25) ◽  
pp. 252902 ◽  
Author(s):  
Sang Mo Yang ◽  
Lucie Mazet ◽  
M. Baris Okatan ◽  
Stephen Jesse ◽  
Gang Niu ◽  
...  
Keyword(s):  
Cross Talk ◽  
Piezoresponse Force Microscopy ◽  
Microscopy Imaging ◽  
Force Microscopy ◽  
Imaging And Spectroscopy

scholarly journals Advances in Atomic Force Microscopy: Imaging of Two- and Three-Dimensional Interfacial Water

2021 ◽  
Vol 9 ◽  
Author(s):  
Duanyun Cao ◽  
Yizhi Song ◽  
BinZe Tang ◽  
Limei Xu
Keyword(s):  
Atomic Force Microscopy ◽  
Dynamic Properties ◽  
Three Dimensional ◽  
Interfacial Water ◽  
Microscopy Imaging ◽  
Force Microscopy ◽  
Atomic Force ◽  
Atomic Force Microscopy Imaging ◽  
Complex Structural ◽  
Many Core

Interfacial water is closely related to many core scientific and technological issues, covering a broad range of fields, such as material science, geochemistry, electrochemistry and biology. The understanding of the structure and dynamics of interfacial water is the basis of dealing with a series of issues in science and technology. In recent years, atomic force microscopy (AFM) with ultrahigh resolution has become a very powerful option for the understanding of the complex structural and dynamic properties of interfacial water on solid surfaces. In this perspective, we provide an overview of the application of AFM in the study of two dimensional (2D) or three dimensional (3D) interfacial water, and present the prospect and challenges of the AFM-related techniques in experiments and simulations, in order to gain a better understanding of the physicochemical properties of interfacial water.

scholarly journals Potential Prepore Trimer Formation by the Bacillus thuringiensis Mosquito-specific Toxin

2015 ◽  
Vol 290 (34) ◽  
pp. 20793-20803 ◽  
Author(s):  
Wilaiwan Sriwimol ◽  
Aratee Aroonkesorn ◽  
Somsri Sakdee ◽  
Chalermpol Kanchanawarin ◽  
Takayuki Uchihashi ◽  
...  
Keyword(s):  
Atomic Force Microscopy ◽  
Bacillus Thuringiensis ◽  
High Speed ◽  
Three Dimensional ◽  
Molecular Assembly ◽  
Microscopy Imaging ◽  
Force Microscopy ◽  
Atomic Force ◽  
Atomic Force Microscopy Imaging ◽  
Trimer Formation

The insecticidal feature of the three-domain Cry δ-endotoxins from Bacillus thuringiensis is generally attributed to their capability to form oligomeric pores, causing lysis of target larval midgut cells. However, the molecular description of their oligomerization process has not been clearly defined. Here a stable prepore of the 65-kDa trypsin-activated Cry4Ba mosquito-specific toxin was established through membrane-mimetic environments by forming an ∼200-kDa octyl-β-d-glucoside micelle-induced trimer. The SDS-resistant trimer caused cytolysis to Sf9 insect cells expressing Aedes-mALP (a Cry4Ba receptor) and was more effective than a toxin monomer in membrane perturbation of calcein-loaded liposomes. A three-dimensional model of toxin trimer obtained by negative-stain EM in combination with single-particle reconstruction at ∼5 nm resolution showed a propeller-shaped structure with 3-fold symmetry. Fitting the three-dimensional reconstructed EM map with a 100-ns molecular dynamics-simulated Cry4Ba structure interacting with an octyl-β-d-glucoside micelle showed relative positioning of individual domains in the context of the trimeric complex with a major protrusion from the pore-forming domain. Moreover, high-speed atomic force microscopy imaging at nanometer resolution and a subsecond frame rate demonstrated conformational transitions from a propeller-like to a globularly shaped trimer upon lipid membrane interactions, implying prepore-to-pore conversion. Real-time trimeric arrangement of monomers associated with l-α-dimyristoylphosphatidylcholine/3-[(3-cholamidopropyl)dimethylammonio]-2-hydroxy-1-propanesulfonic acid bicelle membranes was also envisaged by successive high-speed atomic force microscopy imaging, depicting interactions among three individual subunits toward trimer formation. Together, our data provide the first pivotal insights into the structural requirement of membrane-induced conformational changes of Cry4Ba toxin monomers for the molecular assembly of a prepore trimer capable of inserting into target membranes to generate a lytic pore.

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