Supramolecular assembly system depended on guest species based on bis-naphthane modified β-cyclodextrin dimer

2007 ◽  
Vol 59 (3-4) ◽  
pp. 341-344 ◽  
Author(s):  
Masaya Toda ◽  
Yoshihiko Kondo ◽  
Fumio Hamada
2019 ◽  
Vol 11 (37) ◽  
pp. 4822-4828
Author(s):  
Lan Jia ◽  
Yufang Yang ◽  
Xiang Liu ◽  
Song Chen ◽  
Jingxin Zhu

A novel label-free fluorometric assay for trypsin detection was successfully established on the basis of an anionic sulfonate gemini surfactant C12C3C12(SO3)2/bovine serum albumin (BSA)/nile red (NR) supramolecular assembly system.


Author(s):  
U. Aebi ◽  
R. Millonig ◽  
H. Salvo

To date, most 3-D reconstructions of undecorated actin filaments have been obtained from actin filament paracrystal data (for refs, see 1,2). However, due to the fact that (a) the paracrystals may be several filament layers thick, and (b) adjacent filaments may sustantially interdigitate, these reconstructions may be subject to significant artifacts. None of these reconstructions has permitted unambiguous tracing or orientation of the actin subunits within the filament. Furthermore, measured values for the maximal filament diameter both determined by EM and by X-ray diffraction analysis, vary between 6 and 10 nm. Obviously, the apparent diameter of the actin filament revealed in the EM will critically depend on specimen preparation, since it is a rather flexible supramolecular assembly which can easily be bent or distorted. To resolve some of these ambiguities, we have explored specimen preparation conditions which may preserve single filaments sufficiently straight and helically ordered to be suitable for single filament 3-D reconstructions, possibly revealing molecular detail.


2020 ◽  
Author(s):  
Ian Colliard ◽  
Gregory Morrosin ◽  
Hans-Conrad zur Loye ◽  
May Nyman

Superatoms are nanometer-sized molecules or particles that can form ordered lattices, mimicking their atomic counterparts. Hierarchical assembly of superatoms gives rise to emergent properties in superlattices of quantum-dots, p-block clusters, and fullerenes. Here, we introduce a family of uranium-oxysulfate cluster anions whose hierarchical assembly in water is controlled by two parameters; acidity and the countercation. In acid, larger Ln<sup>III</sup> (Ln=La-Ho) link hexamer (U<sub>6</sub>) oxoclusters into body-centered cubic frameworks, while smaller Ln<sup>III</sup> (Ln=Er-Lu &Y) promote linking of fourteen U<sub>6</sub>-clusters into hollow superclusters (U<sub>84</sub> superatoms). U<sub>84</sub> assembles into superlattices including cubic-closest packed, body-centered cubic, and interpenetrating networks, bridged by interstitial countercations, and U<sub>6</sub>-clusters. Divalent transition metals (TM=Mn<sup>II </sup>and Zn<sup>II</sup>), with no added acid, charge-balance and promote the fusion of 10 U<sub>6</sub> and 10 U-monomers into a wheel–shaped cluster (U<sub>70</sub>). Dissolution of U<sub>70</sub> in organic media reveals (by small-angle Xray scattering) that differing supramolecular assemblies are accessed, controlled by TM-linking of U<sub>70</sub>-clusters. <br>


ROBOT ◽  
2013 ◽  
Vol 35 (5) ◽  
pp. 589
Author(s):  
Dechun ZHENG ◽  
Yongping ZHANG ◽  
Guojun LI

Biology ◽  
2021 ◽  
Vol 10 (4) ◽  
pp. 294
Author(s):  
Thunyarat Surasiang ◽  
Chalongrat Noree

Asparagine synthetase deficiency (ASD) has been found to be caused by certain mutations in the gene encoding human asparagine synthetase (ASNS). Among reported mutations, A6E mutation showed the greatest reduction in ASNS abundance. However, the effect of A6E mutation has not yet been tested with yeast asparagine synthetase (Asn1/2p). Here, we constructed a yeast strain by deleting ASN2 from its genome, introducing the A6E mutation codon to ASN1, along with GFP downstream of ASN1. Our mutant yeast construct showed a noticeable decrease of Asn1p(A6E)-GFP levels as compared to the control yeast expressing Asn1p(WT)-GFP. At the stationary phase, the A6E mutation also markedly lowered the assembly frequency of the enzyme. In contrast to Asn1p(WT)-GFP, Asn1p(A6E)-GFP was insensitive to changes in the intracellular energy levels upon treatment with sodium azide during the log phase or fresh glucose at the stationary phase. Our study has confirmed that the effect of A6E mutation on protein expression levels of asparagine synthetase is common in both unicellular and multicellular eukaryotes, suggesting that yeast could be a model of ASD. Furthermore, A6E mutation could be introduced to the ASNS gene of acute lymphoblastic leukemia patients to inhibit the upregulation of ASNS by cancer cells, reducing the risk of developing resistance to the asparaginase treatment.


Author(s):  
Moretti Emilio ◽  
Tappia Elena ◽  
Limère Veronique ◽  
Melacini Marco

AbstractAs a large number of companies are resorting to increased product variety and customization, a growing attention is being put on the design and management of part feeding systems. Recent works have proved the effectiveness of hybrid feeding policies, which consist in using multiple feeding policies in the same assembly system. In this context, the assembly line feeding problem (ALFP) refers to the selection of a suitable feeding policy for each part. In literature, the ALFP is addressed either by developing optimization models or by categorizing the parts and assigning these categories to policies based on some characteristics of both the parts and the assembly system. This paper presents a new approach for selecting a suitable feeding policy for each part, based on supervised machine learning. The developed approach is applied to an industrial case and its performance is compared with the one resulting from an optimization approach. The application to the industrial case allows deepening the existing trade-off between efficiency (i.e., amount of data to be collected and dedicated resources) and quality of the ALFP solution (i.e., closeness to the optimal solution), discussing the managerial implications of different ALFP solution approaches and showing the potential value stemming from machine learning application.


Sign in / Sign up

Export Citation Format

Share Document