scholarly journals THERMAL STABILITY OF SULFUR-CONTAINING ALDEHYDE POLYMERS AND THERMAL STABILIZATION EFFECT OF THEIR OLIGOMERS

1972 ◽  
Vol 45 (6) ◽  
pp. 582-587 ◽  
Author(s):  
I. Yamashita ◽  
N. Yamamoto ◽  
R. Yamamoto
Keyword(s):  
Thermal Stability ◽  
Thermal Stabilization ◽  
Stabilization Effect ◽  
Sulfur Containing ◽  
Thermal Stability Of

Evaluation of the Thermal Stabilization Effect of Maleic Anhydride Derivatives on Polyvinyl Chloride

2012 ◽  
Vol 535-537 ◽  
pp. 1167-1170
Author(s):  
Jian Ping Liu ◽  
Xia Song ◽  
Wei Yuan ◽  
Xiao Yan Wang
Keyword(s):  
Thermal Stability ◽  
Maleic Anhydride ◽  
Thermal Degradation ◽  
Polyvinyl Chloride ◽  
Color Change ◽  
Thermal Stabilization ◽  
Test Paper ◽  
Stabilization Effect ◽  
Thermal Stability Of

Here, we synthesized a series of polymeric thermal stabilizers for polyvinyl chloride (PVC) based on maleic anhydride derivatives, including N-phenylmaleimide (NPMI), N-p-chlorophenyl maleimide (NCIPMI), N-p-nitrophenyl maleimide (NNOPMI), dibutyltin maleate (DBTM) and dioctyltin maleate (DOTM). Five specimens were prepared by mixing and rolling through a blending machine and a double-roller mixer, respectively. These samples were first subjected to thermal degradation in a 180°C hot oven, and fractions were collected every 10 min, followed by spotting on a slip of test paper. From the degree of color change in the test paper, the influences of these compounds on the thermal stability of PVC were estimated and such mechanisms were also discussed.

The role of glycosylation and domain interactions in the thermal stability of human angiotensin-converting enzyme

2008 ◽  
Vol 389 (9) ◽  
Author(s):  
Hester G. O'Neill ◽  
Pierre Redelinghuys ◽  
Sylva L.U. Schwager ◽  
Edward D. Sturrock
Keyword(s):  
Thermal Stability ◽  
Angiotensin Converting Enzyme ◽  
Physicochemical Properties ◽  
Mammalian Cells ◽  
Insect Cells ◽  
Thermal Stabilization ◽  
Site Directed Mutagenesis ◽  
Converting Enzyme ◽  
Complex Glycans ◽  
Thermal Stability Of

Abstract The N and C domains of somatic angiotensin-converting enzyme (sACE) differ in terms of their substrate specificity, inhibitor profiling, chloride dependency and thermal stability. The C domain is thermally less stable than sACE or the N domain. Since both domains are heavily glycosylated, the effect of glycosylation on their thermal stability was investigated by assessing their catalytic and physicochemical properties. Testis ACE (tACE) expressed in mammalian cells, mammalian cells in the presence of a glucosidase inhibitor and insect cells yielded proteins with altered catalytic and physicochemical properties, indicating that the more complex glycans confer greater thermal stabilization. Furthermore, a decrease in tACE and N-domain N-glycans using site-directed mutagenesis decreased their thermal stability, suggesting that certain N-glycans have an important effect on the protein's thermodynamic properties. Evaluation of the thermal stability of sACE domain swopover and domain duplication mutants, together with sACE expressed in insect cells, showed that the C domain contained in sACE is less dependent on glycosylation for thermal stabilization than a single C domain, indicating that stabilizing interactions between the two domains contribute to the thermal stability of sACE and are decreased in a C-domain-duplicating mutant.

Colorimetric study of thermal stability of sulfur-containing additives

1979 ◽  
Vol 15 (5) ◽  
pp. 384-386
Author(s):  
N. A. Kudryavtseva ◽  
A. A. Fufaev ◽  
S. B. Borshchevskii ◽  
N. I. Lulova
Keyword(s):  
Thermal Stability ◽  
Colorimetric Study ◽  
Sulfur Containing ◽  
Thermal Stability Of

Grain Growth Behaviour Of Nanocrystalline Nickel

1991 ◽  
Vol 238 ◽  
Author(s):  
A. M. El-Sherik ◽  
K. Boylan ◽  
U. Erb ◽  
G. Palumbo ◽  
K. T. Aust
Keyword(s):  
Electron Microscopy ◽  
Thermal Stability ◽  
Grain Size ◽  
Grain Boundary ◽  
Grain Growth ◽  
Thermal Stabilization ◽  
Growth Behaviour ◽  
In Situ Electron Microscopy ◽  
Thermal Stability Of

ABSTRACTThe thermal stability of electrodeposited nanocrystalline Ni-1.2%P and Ni-0.12%S alloys is evaluated by in-situ electron microscopy studies. Isothermal grain size versus annealing time curves at 573K and 623K show an unexpected thermal stabilization in form of a transition from rapid initial grain growth to negligible grain growth. This behaviour is discussed in terms of the various grain boundary drag mechanisms which may be operative in these alloys.

scholarly journals Additivity of the Stabilization Effect of Single Amino Acid Substitutions in Triple Mutants of Recombinant Formate Dehydrogenase from the Soybean Glycine max

Acta Naturae ◽  
2015 ◽  
Vol 7 (3) ◽  
pp. 55-64 ◽  
Author(s):  
A. A. Alekseeva ◽  
I. S. Kargov ◽  
S. Yu. Kleimenov ◽  
S. S. Savin ◽  
V I. Tishkov
Keyword(s):  
Thermal Stability ◽  
Glycine Max ◽  
Amino Acid ◽  
Formate Dehydrogenase ◽  
Single Amino Acid ◽  
Inactivation Kinetics ◽  
Amino Acid Substitutions ◽  
Stabilization Effect ◽  
The Stability ◽  
Thermal Stability Of

Recently, we demonstrated that the amino acid substitutions Ala267Met and Ala267Met/Ile272Val (Alekseeva et al., Biochemistry, 2012), Phe290Asp, Phe290Asn and Phe290Ser (Alekseeva et al., Prot. Eng. Des. Select, 2012) in recombinant formate dehydrogenase from soya Glycine max (SoyFDH) lead to a significant (up to 30-100 times) increase in the thermal stability of the enzyme. The substitutions Phe290Asp, Phe290Asn and Phe290Ser were introduced into double mutant SoyFDH Ala267Met/Ile272Val by site-directed mutagenesis. Combinations of three substitutions did not lead to a noticeable change in the catalytic properties of the mutant enzymes. The stability of the resultant triple mutants was studied through thermal inactivation kinetics and differential scanning calorimetry. The thermal stability of the new mutant SoyFDHs was shown to be much higher than that of their precursors. The stability of the best mutant SoyFDH Ala267Met/Ile272Val/Phe290Asp turned out to be comparable to that of the most stable wild-type formate dehydrogenases from other sources. The results obtained with both methods indicate a great synergistic contribution of individual amino acid substitutions to the common stabilization effect.

Thermal Stability of DNA Interacting with Furazolidone and Cu(II) Ions

1983 ◽  
Vol 38 (3-4) ◽  
pp. 290-293 ◽  
Keyword(s):  
Thermal Stability ◽  
Transition Temperature ◽  
Thermal Stabilization ◽  
Dna Complex ◽  
Thermal Stability Of

Furazolidone, on complexing with DNA, led to its thermal stabilization. The increase in transition temperature of DNA (ΔTm) increased linearly with % A - T content. Increasing concentration of Cu(II) ions progressively lowered the transition tem perature of DNA, but Cu(II) ions were not equally effective in lowering the transition temperature of furazolidone-DNA complex. When equimolar amounts of Cu(II) ions and furazolidone were used, the stabilisation effects of furazolidone prevailed over the destabilisation effect of Cu(II) ions

Evaluation of the Thermal Stabilization Effect of the Bis (Mercaptoethanol Oleate) Dimethyl Tin on Polyvinyl Chloride

2012 ◽  
Vol 581-582 ◽  
pp. 81-84
Author(s):  
Jian Ping Liu ◽  
Hong Zhou Shang ◽  
Xia Song ◽  
Wei Yuan ◽  
Shu Mei Zhou
Keyword(s):  
Polyvinyl Chloride ◽  
Tensile Testing ◽  
Testing Machine ◽  
Thermal Stabilization ◽  
Elongation Rate ◽  
Tensile Testing Machine ◽  
Thermal Stabilities ◽  
Elongation At Break ◽  
Stabilization Effect ◽  
Thermal Stability Of

Bis (mercaptoethanol oleate) dimethyl tin was synthesized and added to polyvinyl chloride (PVC) with various ratios. Specimens were prepared by mixing and rolling through a double-roller mixer, and their static thermal stabilities were estimated by the oven static thermal aging experiments. The influence of the bis (mercaptoethanol oleate) dimethyl tin on the dynamic thermal stability of PVC was tested through a haack torque rheometer (HAAKE PolyLab QC). The tensile strength and rate of elongation at break of the PVC specimens were evaluated by a servo-controlled tensile testing machine. The results show that the bis (mercaptoethanol oleate) dimethyl tin has excellent static and dynamic thermal stabilization effect on PVC, and to some extent, can improve the breaking elongation rate the PVC sample.

scholarly journals Influence of oligoribonucleotides on the conformation and stability of interferon

2020 ◽  
Vol 17 (2) ◽  
pp. 165-171
Author(s):  
R. O. Nikolaiev ◽  
M. M. Vivcharyk ◽  
S. I. Chernykh ◽  
Z. Yu. Tkachuk
Keyword(s):  
Thermal Stability ◽  
Protein Structure ◽  
Specific Binding ◽  
Thermal Stabilization ◽  
Parent Drug ◽  
Protein Molecule ◽  
Interferon Α ◽  
Tertiary Protein Structure ◽  
Quenching Method ◽  
Thermal Stability Of

Aim. To study the ability of yeast RNA oligoribonucleotides (ORNs) and their complexes withD-mannitol to influence the conformation and thermal stability of interferon (INF) α-2b. Methods. The ability of oligoribonucleotide drugs to bind to INF α-2b was studied using its fluorescence quenching method. The effect of ORN drugs on protein stability was studied by analyzing the thermal stability of INF. To confirm their influence on the conformation of the INF, we investigated the spectra of circular dichroism. Results. The ORN complexes with D-mannitol, due to their better protein binding, have been shown to have a much higher effect on the conformation and thermal stability of interferon α-2b than ORN. ORNs and their complexes with D-mannitol also increase the thermal stabilization of interferon. The addition of ORN and ORN with D-mannitol to INF leads to a decrease in the content of α-helical components in the protein structure and an increase in β-components and unstructured parts of the protein molecule. Addition of the ORN complex: D-mannitol, unlike the ORN, changes the architecture of the tertiary INF structure. Conclusions. Therefore, the ORN complexes with D-mannitol have a much higher effect on the conformation and thermal stability of interferon α-2b than the parent drug ORN. The more specific binding of oligonucleotides can probably explain this in the presence of mannitol to the protein. ORNs and ORN complexes with D-mannitol also increase the thermal stabilization of interferon by 2 and 1.8 °C, respectively. The addition of ORNs and ORN complexes with D-mannitol leads to a decrease in the content of α- helical components in the protein structure and an increase in antiparallel β-sheets, β-turns, and unstructured elements. In the presence of mannitol in the ORN molecule, the structure of INF changes more intensively. Addition of ORN complexes: D-mannitol to INF, unlike ORN, changes the architecture of the tertiary protein structure from a 2-layer sandwich to an alpha-beta complex.Keywords: oligonucleotides; interferon; mannitol; secondary protein structure.

scholarly journals Protein thermal stabilization in aqueous solutions of osmolytes.

2015 ◽  
Vol 63 (1) ◽  
Author(s):  
Piotr Bruździak ◽  
Aneta Panuszko ◽  
Muriel Jourdan ◽  
Janusz Stangret
Keyword(s):  
Thermal Stability ◽  
Aqueous Solutions ◽  
Theoretical Calculations ◽  
Thermal Stabilization ◽  
Protein Stabilization ◽  
Hen Egg White Lysozyme ◽  
Egg White Lysozyme ◽  
Hen Egg White ◽  
Thermal Stability Of ◽  
Distinctive Role

Proteins' thermal stabilization is a significant problem in various biomedical, biotechnological, and technological applications. We investigated thermal stability of hen egg white lysozyme in aqueous solutions of the following stabilizing osmolytes: Glycine (GLY), N-methylglycine (NMG), N,N-dimethylglycine (DMG), N,N,N-trimethylglycine (TMG), and trimethyl-N-oxide (TMAO). Results of CD-UV spectroscopic investigation were compared with FTIR hydration studies' results. Selected osmolytes increased lysozyme's thermal stability in the following order: Gly>NMG>TMAO≈DMG>TMG. Theoretical calculations (DFT) showed clearly that osmolytes' amino group protons and water molecules interacting with them played a distinctive role in protein thermal stabilization. The results brought us a step closer to the exact mechanism of protein stabilization by osmolytes.

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