ChemInform Abstract: New Type of 2-Alkyl-substituted 1,8-Naphthyridine Systems Containing a Phosphoryl Group in the Side Chain.

Abstract With epoxycyclohexane as critical modifying monomer, the copolyether was obtained by cationic ring-opening polymerization of epichlorohydrin and epoxycyclohexane. Then biphenyl was used as the mesogen, and diglycolamidic acid was used as the terminal chelating group, a new type of side chain liquid crystal polyether chelating resin was prepared at last. The adsorption influence factors, reuse performance, adsorption model and adsorption kinetics of the chelated resin on Cu 2+ in water were studied systematically. The results showed that the resin has good adsorption and reuse performance for the treatment of Cu 2+ in water, and the adsorption of Cu 2+ is Langmuir monolayer adsorption, and the adsorption process conforms to a quasi-second-order kinetic model. The adsorption performances of the chelated resin has great potential for recovery of copper resource from non-ferrous smelting industry.

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Bacteriochlorophyll e : structure and stereochemistry of a new type of chlorophyll from Chlorobiaceae

Philosophical Transactions of the Royal Society of London Series B Biological Sciences ◽

10.1098/rstb.1976.0013 ◽

1976 ◽

Vol 273 (924) ◽

pp. 277-285 ◽

Cited By ~ 30

Keyword(s):

Nuclear Magnetic Resonance ◽

Oxidative Degradation ◽

Chemical Properties ◽

Structural Formula ◽

Side Chain ◽

Physical And Chemical Properties ◽

New Type ◽

Physical And Chemical ◽

Bacteriochlorophyll E ◽

And Chemical Properties

A so far unknown chlorophyll has been isolated from several strains of brown-coloured chlorobacteria and has been designated bacteriochlorophyll e . Comparison of the physical and chemical properties of the new chlorophyll with those of bacteriochlorophylls c and d ( Chlorbium chlorophylls) allows one to deduce its structural formula. The stereochemistry of the hydroxyethyl side chain of bacteriochlorophylls c, d and e can be determined by a modified Horeau analysis of these pigments, and the results thus obtained are in agreement with those derived from oxidative degradation experiments. The latter method allows one furthermore to prove the structure of bacteriochlorophylls c and d proposed by Holt, and to establish the absolute configuration at carbon atoms 7 and 8. The presence of a δ-methylsubstituent in bacteriochlorophylls c and e is unambiguously demonstrated by nuclear magnetic resonance.

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Oxygen-permselectivity in new type polyorganosiloxanes with carboxyl group on the side chain

Polymer Bulletin ◽

10.1007/bf01033110 ◽

1990 ◽

Vol 23 (6) ◽

pp. 637-642 ◽

Cited By ~ 16

Author(s):

Manshi Ohyanagi ◽

Hiroyuki Nishide ◽

Koichi Suenaga ◽

Eishun Tsuchida

Keyword(s):

Side Chain ◽

Carboxyl Group ◽

New Type

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The structure and function of HPr

Biochemistry and Cell Biology ◽

10.1139/o98-043 ◽

1998 ◽

Vol 76 (2-3) ◽

pp. 359-367 ◽

Cited By ~ 12

Author(s):

E Bruce Waygood

Keyword(s):

Structure And Function ◽

Side Chain ◽

Phosphoryl Group ◽

Phosphotransferase System ◽

Tertiary Structures ◽

E Coli ◽

H Nmr ◽

Early Protein ◽

Alpha Beta ◽

And Function

Histidine-containing phosphocarrier protein, HPr, was one of the early protein tertiary structures determined by two-dimensional 1H-NMR. Tertiary structures for HPrs from Escherichia coli, Bacillus subtilis, and Staphylococcus aureus have been obtained by 1H NMR and the overall folding pattern of HPr is highly conserved, a beta alpha beta beta alpha beta alpha arrangement of three alpha-helices overlaying a four-stranded beta-sheet. High-resolution structures for HPrs from E. coli and B. subtilis have been obtained using 15N- and 13C-labeled proteins. The first application of NMR to the understanding of the structure and function of HPr was to describe the phosphohistidine isomer, Ndelta1-P-histidine in S. aureus phospho-HPr, and the unusual pKas of the His-15 side chain. The pKa values for the His-15 imidazole from more recent studies are 5.4 for HPr and 7.8 for phospho-HPr from E. coli, for example. A consensus description of the active site is proposed for HPr and phospho-HPr. In HPr, His-15 has a defined conformation and N-caps helix A, and is thus affected by the helix dipole. His-15 undergoes a small conformational change upon phosphorylation, a movement to allow the phosphoryl group to be positioned such that it forms hydrogen bonds with the main chain amide nitrogens of residue 16 (not conserved) and Arg-17. Interactions between residue 12 side chain (not conserved: asparagine, serine, and threonine) and His-15, and between the Arg-17 guanidinium group and the phosphoryl group, are either weak or transitory.Key words: HPr, NMR, phosphoenolpyruvate:sugar phosphotransferase system, phosphohistidine, phosphoserine.

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Photo Alignment Behaviour of Polyethene Imine Having Cyano Azobenzene Side Chain

Dhaka University Journal of Science ◽

10.3329/dujs.v63i2.24434 ◽

2015 ◽

Vol 63 (2) ◽

pp. 67-72

Author(s):

Mohammad Kamruzzaman ◽

Seiji Kurihara

Keyword(s):

Molecular Orientation ◽

Uv Light ◽

Side Chain ◽

Reaction Parameters ◽

Reaction Conditions ◽

Out Of Plane ◽

Solid Film ◽

New Type ◽

Photo Alignment ◽

Random State

New type of polyethene imine having cyano (-CN) side chain through six methylene spacer group (PEI6C) was successfully synthesised and characterised. The effect of reaction parameters on degree of substitution of PEI6C was also studied and the reaction conditions were optimised. Photochemical as well as photoorientational behaviour of the polymer were investigated. PEI6C in solid film exhibited photoresponsive properties upon irradiation with UV and visible light. PEI6C film also exhibited reversible molecular orientation from random state to out-of-plane and from out-of-plane to random state upon non-polarised visible and UV light irradiation.Dhaka Univ. J. Sci. 63(2): 67-72, 2015 (July)

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The governor: Protein phosphorylation

The Biochemist ◽

10.1042/bio02904020 ◽

2007 ◽

Vol 29 (4) ◽

pp. 20-23 ◽

Cited By ~ 1

Author(s):

Dario R. Alessi and Elton Zeqiraj

Keyword(s):

Protein Phosphorylation ◽

Protein Molecule ◽

Side Chain ◽

Phosphoryl Group ◽

Biological Processes ◽

Eukaryotic Organisms ◽

Almost All

At first glance, the odds that the introduction of a diminutive and unsuspicious phosphoryl group on to a hydroxycontaining side chain of a much larger protein molecule would be selected by Nature as the most widely deployed mechanism to control biological processes, and be responsible for many major diseases, seems unlikely. However, this process termed protein phosphorylation is a vital regu lator of almost all events that take place in eukaryotic organisms. In this review we will outline what phosphorylation is, how it is regulated and why disruptions of the network of enzymes and proteins that regulate the phosphorylation are a principal cause of many maladies. We will also discuss how advances are leading to exciting strategies to develop drugs to treat diseases caused by disruptions of protein phosphorylation.

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Synthesis of a New Type of Trans-Decalin Vitamin D Analogue through a Dyotropic Ring Expansion

Journal of Chemistry ◽

10.1155/2021/6429427 ◽

2021 ◽

Vol 2021 ◽

pp. 1-5

Author(s):

Hugo Santalla ◽

Uxía Gómez-Bouzó ◽

Irene Sánchez-Sanz ◽

Yagamare Fall

Keyword(s):

Vitamin D ◽

Research Group ◽

Ring Expansion ◽

Ring System ◽

Side Chain ◽

Sulphur Atom ◽

Mild Conditions ◽

New Type ◽

Vitamin D Analogue

A new vitamin D analogue with a trans-fused decalin as the CD-ring system and containing a sulphur atom in the side chain has been synthesized in our research group. The obtention of this analogue is based on a recently discovered transformation of hydrindane cores into decalins through a dyotropic ring expansion in very mild conditions.

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The study on polycarboxylate superplasticizer with polyamine side chain using molecular dynamics simulation

Journal of Physics Conference Series ◽

10.1088/1742-6596/2133/1/012013 ◽

2021 ◽

Vol 2133 (1) ◽

pp. 012013

Author(s):

Xiaochen Lin ◽

Pohsiang Chuang ◽

Yunhui Fang

Keyword(s):

Molecular Dynamics ◽

Aqueous Solution ◽

Molecular Dynamics Simulation ◽

Linear Structure ◽

Reducing Agent ◽

Dynamics Simulation ◽

Side Chain ◽

Water Molecules ◽

Migration Ability ◽

New Type

Abstract A new type of water-reducing agent, which contains polyamine side chains, has been theoretically studied utilizing molecular dynamics simulation (MD) in this research. The models of three types of water reducers in an aqueous solution, including SNF, PCE, and PCA, have been constructed, simulated, and analyzed. The results indicate that compared to the linear structure of SNF, the traditional PCE water-reducing agent has a stronger interaction with water molecules, so it has a better water-reducing effect. This stronger interaction is mainly provided by the side chain of PCE. PCA further enhances the hydrophilicity of its side chain based on PCE structure, leading to a stronger interaction on water molecules than traditional PCE molecules. The migration ability of water-reducing agents and other molecules in the system has been further explored. The diffusion coefficient of three water reducer molecules decreases in the following order: PCE>SNF>PCA. This is due to the interaction between molecules, especially the incompatible strength and quantity of hydrogen bonding.

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Fibrinogen Mitaka II: a hereditary dysfibrinogen with defective thrombin binding caused by an A alpha Glu-11 to Gly substitution

Blood ◽

10.1182/blood.v82.12.3658.3658 ◽

1993 ◽

Vol 82 (12) ◽

pp. 3658-3663 ◽

Cited By ~ 12

Author(s):

K Niwa ◽

A Yaginuma ◽

M Nakanishi ◽

Y Wada ◽

T Sugo ◽

...

Keyword(s):

High Performance ◽

Salt Bridge ◽

Side Chain ◽

Fibrinopeptide A ◽

Beta Turn ◽

Fibrin Gels ◽

Local Conformation ◽

New Type ◽

Guanidino Group ◽

Normal Controls

Abstract A new type of A alpha Glu-11 to Gly substitution has been identified in a congenitally abnormal fibrinogen, fibrinogen Mitaka II, derived from a 14-year-old female suffering from easy bruising since childhood. Plasma of the patient and fibrinogen purified therefrom were found to clot slowly by thrombin but in a normal fashion by ancrod, a thrombin- like snake venom enzyme. The ancrod-clotted fibrin gels were normally solid and turbid, whereas the thrombin-clotted gels were initially fragile and transparent but became gradually normalized during further incubation. On reverse-phase high-performance liquid chromatography, there was an additional peptide group eluted distinctly later than the corresponding normal fibrinopeptide A in the clot-liquor of the patient's samples. Sequence analysis of these aberrant peptides and isolated A alpha chains of the patient's fibrinogen showed that Glu at position 11 of the abnormal A alpha chain had been replaced by Gly. Studies using 125I-labeled thrombin showed that the binding with thrombin was evidently reduced for her fibrinogen and the aberrant fibrinopeptide A as compared with that for the normal controls, indicating that A alpha Glu-11 may be critical for the fibrinogen- thrombin interaction. Indeed, A alpha Glu-11 of fibrinogen has recently been proposed to stabilize the local conformation, including the beta- turn, and to form a salt bridge between its side-chain carboxyl group and the guanidino group of Arg-173 of thrombin based on crystallographic analyses using analogs of fibrinopeptide A complexed with thrombin (Stubb et al, Eur J Biochem 206:187, 1992 and Martin et al, J Biol Chem 267:7911, 1992).

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