Symmetry Breaking in the Self-Assembly of Partially Fluorinated Benzene-1,3,5-tricarboxamides

2012 ◽  
Vol 51 (45) ◽  
pp. 11297-11301 ◽  
Author(s):  
Patrick J. M. Stals ◽  
Peter A. Korevaar ◽  
Martijn A. J. Gillissen ◽  
Tom F. A. de Greef ◽  
Carel F. C. Fitié ◽  
...  
1996 ◽  
Vol 43 (5) ◽  
pp. 419-424 ◽  
Author(s):  
Stephen J. Sowerby ◽  
Wolfgang M. Heckl ◽  
George B. Petersen

Nanoscale ◽  
2016 ◽  
Vol 8 (5) ◽  
pp. 2951-2959 ◽  
Author(s):  
Xiang-Dong Tian ◽  
Shu Chen ◽  
Yue-Jiao Zhang ◽  
Jin-Chao Dong ◽  
Rajapandiyan Panneerselvam ◽  
...  

The self-assembly of asymmetric nanostructures with adjustable building blocks (Au nanospheres: 90–250 nm and Ag nanocubes: 100–160 nm) and meanwhile with interparticle gaps controlled by silica shells (from 1 nm to beyond 10 nm).


Symmetry ◽  
2019 ◽  
Vol 11 (8) ◽  
pp. 950 ◽  
Author(s):  
Yutao Sang ◽  
Minghua Liu

The origin of biological homochirality, e.g., life selects the L-amino acids and D-sugar as molecular component, still remains a big mystery. It is suggested that mirror symmetry breaking plays an important role. Recent researches show that symmetry breaking can also occur at a supramolecular level, where the non-covalent bond was crucial. In these systems, equal or unequal amount of the enantiomeric nanoassemblies could be formed from achiral molecules. In this paper, we presented a brief overview regarding the symmetry breaking from dispersed system to gels, solids, and at interfaces. Then we discuss the rational manipulation of supramolecular chirality on how to induce and control the homochirality in the self-assembly system. Those physical control methods, such as Viedma ripening, hydrodynamic macro- and micro-vortex, superchiral light, and the combination of these technologies, are specifically discussed. It is hoped that the symmetry breaking at a supramolecular level could provide useful insights into the understanding of natural homochirality and further designing as well as controlling of functional chiral materials.


2012 ◽  
Vol 124 (45) ◽  
pp. 11459-11463 ◽  
Author(s):  
Patrick J. M. Stals ◽  
Peter A. Korevaar ◽  
Martijn A. J. Gillissen ◽  
Tom F. A. de Greef ◽  
Carel F. C. Fitié ◽  
...  

1996 ◽  
Vol 43 (5) ◽  
pp. 419-424
Author(s):  
Stephen J. Sowerby ◽  
Wolfgang M. Heckl ◽  
George B. Petersen

Author(s):  
M. Kessel ◽  
R. MacColl

The major protein of the blue-green algae is the biliprotein, C-phycocyanin (Amax = 620 nm), which is presumed to exist in the cell in the form of distinct aggregates called phycobilisomes. The self-assembly of C-phycocyanin from monomer to hexamer has been extensively studied, but the proposed next step in the assembly of a phycobilisome, the formation of 19s subunits, is completely unknown. We have used electron microscopy and analytical ultracentrifugation in combination with a method for rapid and gentle extraction of phycocyanin to study its subunit structure and assembly.To establish the existence of phycobilisomes, cells of P. boryanum in the log phase of growth, growing at a light intensity of 200 foot candles, were fixed in 2% glutaraldehyde in 0.1M cacodylate buffer, pH 7.0, for 3 hours at 4°C. The cells were post-fixed in 1% OsO4 in the same buffer overnight. Material was stained for 1 hour in uranyl acetate (1%), dehydrated and embedded in araldite and examined in thin sections.


Author(s):  
Xiaorong Zhu ◽  
Richard McVeigh ◽  
Bijan K. Ghosh

A mutant of Bacillus licheniformis 749/C, NM 105 exhibits some notable properties, e.g., arrest of alkaline phosphatase secretion and overexpression and hypersecretion of RS protein. Although RS is known to be widely distributed in many microbes, it is rarely found, with a few exceptions, in laboratory cultures of microorganisms. RS protein is a structural protein and has the unusual properties to form aggregate. This characteristic may have been responsible for the self assembly of RS into regular tetragonal structures. Another uncommon characteristic of RS is that enhanced synthesis and secretion which occurs when the cells cease to grow. Assembled RS protein with a tetragonal structure is not seen inside cells at any stage of cell growth including cells in the stationary phase of growth. Gel electrophoresis of the culture supernatant shows a very large amount of RS protein in the stationary culture of the B. licheniformis. It seems, Therefore, that the RS protein is cotranslationally secreted and self assembled on the envelope surface.


MRS Advances ◽  
2020 ◽  
Vol 5 (64) ◽  
pp. 3507-3520
Author(s):  
Chunhui Dai ◽  
Kriti Agarwal ◽  
Jeong-Hyun Cho

AbstractNanoscale self-assembly, as a technique to transform two-dimensional (2D) planar patterns into three-dimensional (3D) nanoscale architectures, has achieved tremendous success in the past decade. However, an assembly process at nanoscale is easily affected by small unavoidable variations in sample conditions and reaction environment, resulting in a low yield. Recently, in-situ monitored self-assembly based on ion and electron irradiation has stood out as a promising candidate to overcome this limitation. The usage of ion and electron beam allows stress generation and real-time observation simultaneously, which significantly enhances the controllability of self-assembly. This enables the realization of various complex 3D nanostructures with a high yield. The additional dimension of the self-assembled 3D nanostructures opens the possibility to explore novel properties that cannot be demonstrated in 2D planar patterns. Here, we present a rapid review on the recent achievements and challenges in nanoscale self-assembly using electron and ion beam techniques, followed by a discussion of the novel optical properties achieved in the self-assembled 3D nanostructures.


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