Modeling the Self-Assembly of Organic Molecules in 2D Molecular Layers with Different Structures

2015 ◽  
Vol 120 (1) ◽  
pp. 318-323 ◽  
Author(s):  
Joost van der Lit ◽  
Jolien L. Marsman ◽  
Rik S. Koster ◽  
Peter H. Jacobse ◽  
Stephan A. den Hartog ◽  
...  
2002 ◽  
Vol 11 ◽  
pp. 179-194
Author(s):  
David W. Deamer

Movies are the myths of late-20th century western culture. Because of the power of films likeETto capture our imagination, we are more likely than past generations to accept the possibility that life exists elsewhere in our galaxy. Such a myth can be used to sketch the main themes of this chapter, which concern the origin of life on the Earth.


RSC Advances ◽  
2016 ◽  
Vol 6 (75) ◽  
pp. 71638-71651 ◽  
Author(s):  
Ankita Saini ◽  
K. R. Justin Thomas

The self-assembly of small organic molecules into molecular stacks plays a vital role in the construction of stable supramolecular structures.


2016 ◽  
Vol 23 (06) ◽  
pp. 1650047
Author(s):  
XIN SONG ◽  
HUIHUI KONG ◽  
LACHENG LIU ◽  
XIAOQING LIU ◽  
MINGDONG DONG ◽  
...  

It is still a challenge to find a suitable method to fabricate a well-defined homochiral surface from achiral molecules, and one of the possible methods is to modify surfaces with organic molecular assemblies. Large-area chiral self-assembly nanostructures have been observed at room temperature by depositing ZnPc molecules on a Cu(111) surface. The growth process has been investigated. ZnPc molecules get adsorbed first at the terrace steps, and then extend over the lower terrace until the whole terrace is covered with ZnPc molecules; such growth process would be stopped when the self-assembly nanostructure run into a decorated upper terrace step edge. We found that the terrace steps with specific directions with respect to the close-packed directions of the substrate can induce homochiral self-assembly on the lower terraces. So we can propose a possible way to fabricate a well-defined homochiral surface from achiral organic molecules.


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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