Hydrophobic domain structure of water-soluble block copolymer. 1. Analysis of the structure of the polymolecular micelle

1981 ◽  
Vol 14 (1) ◽  
pp. 34-39 ◽  
Author(s):  
Masahisa Ikemi ◽  
Nobuyuki Odagiri ◽  
Shinobu Tanaka ◽  
Isao Shinohara ◽  
Akio Chiba
1982 ◽  
Vol 15 (2) ◽  
pp. 281-286 ◽  
Author(s):  
Masahisa Ikemi ◽  
Nobuyuki Odagiri ◽  
Shinobu Tanaka ◽  
Isao Shinohara ◽  
Akio Chiba

2020 ◽  
Vol 11 (18) ◽  
pp. 3209-3216 ◽  
Author(s):  
Joydeb Mandal ◽  
Andrea Arcifa ◽  
Nicholas D. Spencer

Block-copolymer brushes of water-soluble acrylamides have been synthesised by SI-ATRP under continuous flow and their growth monitored in situ by means of a quartz-crystal microbalance with dissipation (QCM-D).


2014 ◽  
Vol 900 ◽  
pp. 15-19 ◽  
Author(s):  
Xing Lei ◽  
Gui Long Xu ◽  
Jin Yang ◽  
Jian Hu

Water-soluble phenolic resin was prepared using sodium hydroxide and ammonia as catalysts. The molecular structure of water-soluble phenolic with different molecular weight was studied by infrared spectrum and the mechanism was discussed. The results show that addition reaction and polycondensation synchronize in the reaction process, while addition reaction dominates in the early stage while polycondensation dominates in the later stage.


2013 ◽  
Vol 42 (35) ◽  
pp. 12733 ◽  
Author(s):  
Susanne Leubner ◽  
Soheil Hatami ◽  
Nehir Esendemir ◽  
Tommy Lorenz ◽  
Jan-Ole Joswig ◽  
...  

2015 ◽  
Vol 814 ◽  
pp. 220-229
Author(s):  
Hong Xu Zhang ◽  
Yu Jie Zhao ◽  
Jia Zhuang ◽  
Hai Yang Qin ◽  
Han Ling Zhang

With an analysis on the structure of water-soluble sodium silicate and its polymerization, it was found that the poor stability of silicate drilling fluids lies in the relevance between the inherent nature and the pH value of sodium silicate. The modification of water-soluble sodium silicate in this paper was to improve its stability and keep the inhibitive property simultaneously. The a-olefin sulfonate (AOS) was employed as the modifer agent acted on the water-soluble sodium silicate monomer and oligomers. Furthermore, the modification mechanism was discussed through FTIR, Laser particle size, Zeta potential and SEM. A stable sodium silicate drilling fluids with better inhibitive property was obtained by the comparison of modified sodium silicate and unmodified ones.


2009 ◽  
Vol 47 (23) ◽  
pp. 6619-6629 ◽  
Author(s):  
A. L. Nielsen ◽  
M. B. O. Andersen ◽  
T. V. Bugge ◽  
C. F. Nielsen ◽  
T. B. Nielsen ◽  
...  

1989 ◽  
Vol 177 ◽  
Author(s):  
H. Henning Winter ◽  
Faith A. Morrison

Flow can transfer the microphase separated morphology of block copolymers into a state of global order. For tri-block copolymers with cylindrical domains, this has been demonstrated by Folkes et al. (1973) and Hadziioannou et al. (1979). who established the existence of ‘single crystals’ of hexagonally ordered cylinders with uniform director throughout a sheared sample. The director is aligned with the shear direction. In this study, we investigate the flow induced ordering of cylindrical domain structure at increasing levels of shear.


1996 ◽  
Vol 319 (2) ◽  
pp. 411-420 ◽  
Author(s):  
Torben ØSTERLUND ◽  
Birgitta DANIELSSON ◽  
Eva DEGERMAN ◽  
Juan Antonio CONTRERAS ◽  
Gudrun EDGREN ◽  
...  

Hormone-sensitive lipase (HSL) plays a key role in lipid metabolism and overall energy homoeostasis, by controlling the release of fatty acids from stored triglycerides in adipose tissue. Lipases and esterases form a protein superfamily with a common structural fold, called the α/β-hydrolase fold, and a catalytic triad of serine, aspartic or glutamic acid and histidine. Previous alignments between HSL and lipase 2 of Moraxella TA144 have been extended to cover a much larger part of the HSL sequence. From these extended alignments, possible sites for the catalytic triad and α/β-hydrolase fold are suggested. Furthermore, it is proposed that HSL contains a structural domain with catalytic capacity and a regulatory module attached, as well as a structural N-terminal domain unique to this enzyme. In order to test the proposed domain structure, rat HSL was overexpressed and purified to homogeneity using a baculovirus/insect-cell expression system. The purification, resulting in > 99% purity, involved detergent solubilization followed by anion-exchange chromatography and hydrophobic-interaction chromatography. The purified recombinant enzyme was identical to rat adipose-tissue HSL with regard to specific activity, substrate specificity and ability to serve as a substrate for cAMP-dependent protein kinase. The recombinant HSL was subjected to denaturation by guanidine hydrochloride and limited proteolysis. These treatments resulted in more extensive loss of activity against phospholipid-stabilized lipid substrates than against water-soluble substrates, suggesting that the hydrolytic activity can be separated from recognition of lipid substrates. These data support the concept that HSL has at least two major domains.


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