Orientated Attachment Assisted Self-Assembly of Sb2O3 Nanorods and Nanowires:  End-to-End versus Side-by-Side

2007 ◽  
Vol 111 (14) ◽  
pp. 5325-5330 ◽  
Author(s):  
Zhengtao Deng ◽  
Dong Chen ◽  
Fangqiong Tang ◽  
Xianwei Meng ◽  
Jun Ren ◽  
...  
Keyword(s):  
2017 ◽  
Vol 5 (36) ◽  
pp. 7583-7590 ◽  
Author(s):  
Debasish Podder ◽  
Santu Bera ◽  
Mintu Debnath ◽  
Tanmay Das ◽  
Debasish Haldar

An α–α corner mimetic self-assembles into a rod shape supramolecular structure which bends and closes end-to-end like a cyclization reaction to form toroids.


2012 ◽  
Vol 102 (7) ◽  
pp. 1617-1626 ◽  
Author(s):  
Paolo Arosio ◽  
Marta Owczarz ◽  
Hua Wu ◽  
Alessandro Butté ◽  
Massimo Morbidelli

2016 ◽  
Vol 55 (6) ◽  
pp. 2083-2086 ◽  
Author(s):  
Yuki Taniguchi ◽  
Takao Takishita ◽  
Tsuyoshi Kawai ◽  
Takuya Nakashima

2020 ◽  
Vol 10 (1) ◽  
Author(s):  
Pankaj Sharma ◽  
Rachana Tomar ◽  
Shivpratap Singh Yadav ◽  
Maulik D. Badmalia ◽  
Samir Kumar Nath ◽  
...  

AbstractIt remains undeciphered how thermophilic enzymes display enhanced stability at elevated temperatures. Taking l-asparaginase from P. furiosus (PfA) as an example, we combined scattering shapes deduced from small-angle X-ray scattering (SAXS) data at increased temperatures with symmetry mates from crystallographic structures to find that heating caused end-to-end association. The small contact point of self-binding appeared to be enabled by a terminal short β-strand in N-terminal domain, Leu179-Val-Val-Asn182 (LVVN). Interestingly, deletion of this strand led to a defunct enzyme, whereas suplementation of the peptide LVVN to the defunct enzyme restored structural frameworkwith mesophile-type functionality. Crystal structure of the peptide-bound defunct enzyme showed that one peptide ispresent in the same coordinates as in original enzyme, explaining gain-of lost function. A second peptide was seen bound to the protein at a different location suggesting its possible role in substrate-free molecular-association. Overall, we show that the heating induced self-assembly of native shapes of PfA led to an apparent super-stable assembly.


2016 ◽  
Vol 128 (6) ◽  
pp. 2123-2126 ◽  
Author(s):  
Yuki Taniguchi ◽  
Takao Takishita ◽  
Tsuyoshi Kawai ◽  
Takuya Nakashima

2005 ◽  
Vol 16 (9) ◽  
pp. 1776-1780 ◽  
Author(s):  
Bifeng Pan ◽  
Limei Ao ◽  
Feng Gao ◽  
Hongye Tian ◽  
Rong He ◽  
...  

RSC Advances ◽  
2017 ◽  
Vol 7 (23) ◽  
pp. 13896-13903 ◽  
Author(s):  
Lin Chang ◽  
Younas Khan ◽  
Lidong Li ◽  
Nan Yang ◽  
Penggang Yin ◽  
...  

Simple, less time consuming and sensitive self-assembly and colorimetric detection of HVA.


Author(s):  
Shan-Shan Liu ◽  
Shuai Yuan ◽  
Hai-Feng Lu ◽  
Meng-Zhen Xu ◽  
Di Sun

The cation-templated self-assembly of 1,4-bis(2-methyl-1H-imidazol-1-yl)butane (bmimb) with CuSCN gives rise to a novel two-dimensional network, namelycatena-poly[2,2′-dimethyl-1,1′-(butane-1,4-diyl)bis(1H-imidazol-3-ium) [tetra-μ2-thiocyanato-κ4S:S;κ4S:N-dicopper(I)]], {(C12H20N4)[Cu2(NCS)4]}n. The CuIcation is four-coordinated by one N and three S atoms, giving a tetrahedral geometry. One of the two crystallographically independent SCN−anions acts as a μ2-S:Sbridge, binding a pair of CuIcations into a centrosymmetric [Cu2(NCS)2] subunit, which is further extended into a two-dimensional 44-sql net by another kind of SCN−anion with an end-to-end μ2-S:Ncoordination mode. Interestingly, each H2bmimb dication, lying on an inversion centre, threads through one of the windows of the two-dimensional 44-sql net, giving a pseudorotaxane-like structure. The two-dimensional 44-sql networks are packed into the resultant three-dimensional supramolecular framework through bmimb–SCN N—H...N hydrogen bonds.


Catalysts ◽  
2019 ◽  
Vol 9 (9) ◽  
pp. 723
Author(s):  
Kadiri ◽  
Alarcón-Correa ◽  
Ruppert ◽  
Günther ◽  
Bill ◽  
...  

Enzyme-based biocatalysis exhibits multiple advantages over inorganic catalysts, including the biocompatibility and the unchallenged specificity of enzymes towards their substrate. The recovery and repeated use of enzymes is essential for any realistic application in biotechnology, but is not easily achieved with current strategies. For this purpose, enzymes are often immobilized on inorganic scaffolds, which could entail a reduction of the enzymes’ activity. Here, we show that immobilization to a nano-scaled biological scaffold, a nanonetwork of end-to-end cross-linked M13 bacteriophages, ensures high enzymatic activity and at the same time allows for the simple recovery of the enzymes. The bacteriophages have been genetically engineered to express AviTags at their ends, which permit biotinylation and their specific end-to-end self-assembly while allowing space on the major coat protein for enzyme coupling. We demonstrate that the phages form nanonetwork structures and that these so-called nanonets remain highly active even after re-using the nanonets multiple times in a flow-through reactor.


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