Polymer Formation

2014 ◽  
pp. 127-206 ◽  
Keyword(s):  
Polymer Formation

scholarly journals Supramolecular polymer formation by cyclic dinucleotides and intercalators affects dinucleotide enzymatic processing

2016 ◽  
Vol 2 (1) ◽  
Author(s):  
Shizuka Nakayama ◽  
Jie Zhou ◽  
Yue Zheng ◽  
Henryk Szmacinski ◽  
Herman O Sintim
Keyword(s):  
Supramolecular Polymer ◽  
Polymer Formation ◽  
Cyclic Dinucleotides

A New Hydrocarbon Elastomer. I. Copolymerization of Olefins and Nonconjugated Dienes

1962 ◽  
Vol 35 (4) ◽  
pp. 1114-1125 ◽  
Author(s):  
E. K. Gladding ◽  
B. S. Fisher ◽  
J. W. Collette
Keyword(s):  
Oxidative Stability ◽  
Polymer Synthesis ◽  
Laboratory Scale ◽  
Polymer Composition ◽  
Polymerization Temperature ◽  
General Terms ◽  
Polymer Formation ◽  
Polymer Properties ◽  
Catalyst Type

Abstract The composition of sulfur-curable elastomers derived from olefins and diolefins is described and methods are given for their synthesis using coordination catalysts. Certain factors that influence the laboratory-scale polymer synthesis are discussed and the effects of catalyst type, polymerization temperature, and diene structure on the rate of polymer formation and polymer composition are outlined. Polymer properties are discussed in general terms, with particular emphasis on oxidative stability.

Contributions of the structural domains of filensin in polymer formation and filament distribution

1996 ◽  
Vol 109 (2) ◽  
pp. 447-456
Author(s):  
G. Goulielmos ◽  
S. Remington ◽  
F. Schwesinger ◽  
S.D. Georgatos ◽  
F. Gounari
Keyword(s):  
De Novo ◽  
Chimeric Proteins ◽  
Tail Domain ◽  
Structural Domains ◽  
Filament Assembly ◽  
Polymer Formation ◽  
Filament Bundles ◽  
Specific Contribution ◽  
Mcf 7

Filensin and phakinin constitute the subunits of a heteropolymeric, lens-specific intermediate filament (IF) system known as the beaded-chain filaments (BFs). Since the rod of filensin is four heptads shorter than the rods of all other IF proteins, we decided to examine the specific contribution of this protein in filament assembly. For these purposes, we constructed chimeric proteins in which regions of filensin were exchanged with the equivalent ones of vimentin, a self-polymerizing IF protein. Our in vitro studies show that the filensin rod domain does not allow homopolymeric filament elongation. However, the filensin rod is necessary for co-polymerization of filensin with phakinin and seems to counteract the inherent tendency of the latter protein to homopolymerize into large, laterally associated filament bundles. Apart from the rod domain, the presence of an authentic or substituted tail domain in filensin is also essential for co-assembly with the naturally tail-less phakinin and formation of extended filaments in vitro. Finally, transfection experiments in CHO and MCF-7 cells show that the rod domain of filensin plays an important role in de novo filament formation and distribution. The same type of analysis further suggests that the end-domains of filensin interact with cell-specific, assembly-modulating factors.

scholarly journals Evolution of polymer formation within the actin superfamily

2017 ◽  
Vol 28 (19) ◽  
pp. 2461-2469 ◽  
Author(s):  
Patrick R. Stoddard ◽  
Tom A. Williams ◽  
Ethan Garner ◽  
Buzz Baum
Keyword(s):  
Convergent Evolution ◽  
Atp Hydrolysis ◽  
Linear Polymers ◽  
Related Protein ◽  
Protein Families ◽  
Structure And Dynamics ◽  
Polymer Formation ◽  
Filament Structure ◽  
Related Proteins ◽  
Actin Superfamily

While many are familiar with actin as a well-conserved component of the eukaryotic cytoskeleton, it is less often appreciated that actin is a member of a large superfamily of structurally related protein families found throughout the tree of life. Actin-related proteins include chaperones, carbohydrate kinases, and other enzymes, as well as a staggeringly diverse set of proteins that use the energy from ATP hydrolysis to form dynamic, linear polymers. Despite differing widely from one another in filament structure and dynamics, these polymers play important roles in ordering cell space in bacteria, archaea, and eukaryotes. It is not known whether these polymers descended from a single ancestral polymer or arose multiple times by convergent evolution from monomeric actin-like proteins. In this work, we provide an overview of the structures, dynamics, and functions of this diverse set. Then, using a phylogenetic analysis to examine actin evolution, we show that the actin-related protein families that form polymers are more closely related to one another than they are to other nonpolymerizing members of the actin superfamily. Thus all the known actin-like polymers are likely to be the descendants of a single, ancestral, polymer-forming actin-like protein.

scholarly journals Deciphering the role of trehalose in hindering antithrombin polymerization

2019 ◽  
Vol 39 (4) ◽  
Author(s):  
Asma Naseem ◽  
Mohammad Sazzad Khan ◽  
Hashim Ali ◽  
Irshad Ahmad ◽  
Mohamad Aman Jairajpuri
Keyword(s):  
Conformational Change ◽  
Large Scale ◽  
Guanidine Hydrochloride ◽  
Microscopic Analysis ◽  
Normal Activity ◽  
Significant Loss ◽  
Coagulation Cascade ◽  
Disulfonic Acid ◽  
Electron Microscopic ◽  
Polymer Formation

Abstract Serine protease inhibitors (serpins) family have a complex mechanism of inhibition that requires a large scale conformational change. Antithrombin (AT), a member of serpin superfamily serves as a key regulator of the blood coagulation cascade, deficiency of which leads to thrombosis. In recent years, a handful of studies have identified small compounds that retard serpin polymerization but abrogated the normal activity. Here, we screened small molecules to find potential leads that can reduce AT polymer formation. We identified simple sugar molecules that successfully blocked polymer formation without a significant loss of normal activity of AT under specific buffer and temperature conditions. Of these, trehalose proved to be most promising as it showed a marked decrease in the bead like polymeric structures of AT shown by electron microscopic analysis. A circular dichroism (CD) analysis indicated alteration in the secondary structure profile and an increased thermal stability of AT in the presence of trehalose. Guanidine hydrochloride (GdnHCl)-based unfolding studies of AT show the formation of a different intermediate in the presence of trehalose. A time-dependent fluorescence study using 1,1′-bi(4-anilino)naphthalene-5,5′-disulfonic acid (Bis-ANS) shows that trehalose affects the initial conformational change step in transition from native to polymer state through its binding to exposed hydrophobic residues on AT thus making AT less polymerogenic. In conclusion, trehalose holds promise by acting as an initial scaffold that can be modified to design similar compounds with polymer retarding propensity.

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