Stability of Diels–Alder photoadducts in macromolecules

2018 ◽  
Vol 9 (28) ◽  
pp. 3850-3854 ◽  
Author(s):  
Charlotte Petit ◽  
Lukas D. Bangert ◽  
Mahdi Abbasi ◽  
Manfred Wilhelm ◽  
Anja S. Goldmann ◽  
...  
Keyword(s):  
Thermal Stability ◽  
Soft Matter ◽  
Molecular Level ◽  
Diels Alder ◽  
Thermal Stability Of

The study investigates the thermal stability of ligation points resulting from photochemically induced Diels–Alder reactions within soft matter materials on the molecular level.

Microstructure and thermal stability of amorphous materials in the GeS2−La2S3 system

1991 ◽  
Vol 6 (12) ◽  
pp. 2694-2700 ◽  
Author(s):  
Prashant N. Kumta ◽  
Subhash H. Risbud
Keyword(s):  
Thermal Stability ◽  
Amorphous Materials ◽  
Fiber Optic ◽  
Molecular Level ◽  
Infrared Region ◽  
Mid Infrared ◽  
Heat Treated ◽  
Stable Glasses ◽  
Microstructural Studies ◽  
Thermal Stability Of

GeS2 is known to be a good chalcogenide glass former with a transmission cutoff at 11 μm and has been studied for fiber optic application in the mid infrared region. The rare earth sulfides, oxysulfides, and oxides (La–Er) form reasonably good and stable glasses when mixed with chalcogenides such as Ga2S3. In this work, glass formation was studied in the GeS2−La2S3 system. Two compositions containing 60 mol % and 92.5 mol % GeS2, respectively, were analyzed, and the effects of composition on the microstructure and thermal stability of these glasses were investigated. Microstructural studies were conducted on the as-prepared and heat-treated glasses using TEM and SEM/EDXA. Glasses rich in GeS2 exhibited primary (6–88 nm) and secondary (3–13 nm) phase separation at the molecular level. Differential thermal analysis performed on these glasses indicated glass transition temperatures (Tg) of 510 °C and 420 °C for the two compositions studied. The glasses were stable and the (Tg) was observed to decrease with increasing contents of GeS2 in these glasses.

scholarly journals Improved Insights into Protein Thermal Stability: From the Molecular to the Structurome Scale

2016 ◽  
Author(s):  
Fabrizio Pucci ◽  
Marianne Rooman
Keyword(s):  
Thermal Stability ◽  
Amino Acid ◽  
Protein Stability ◽  
Large Scale ◽  
Molecular Level ◽  
Temperature Dependent ◽  
Natural Evolution ◽  
Multi Scale ◽  
Large Scale Analysis ◽  
Thermal Stability Of

AbstractDespite the intense efforts of the last decades to understand the thermal stability of proteins, the mechanisms responsible for its modulation still remain debated. In this investigation, we tackle this issue by showing how a multi-scale perspective can yield new insights. With the help of temperature-dependent statistical potentials, we analyzed some amino acid interactions at the molecular level, which are suggested to be relevant for the enhancement of thermal resistance. We then investigated the thermal stability at the protein level by quantifying its modification upon amino acid substitutions. Finally, a large scale analysis of protein stability - at the structurome level - contributed to the clarification of the relation between stability and natural evolution, thereby showing that the mutational profile of thermostable and mesostable proteins differ. Some final considerations on how the multi-scale approach could help unraveling the protein stability mechanisms are briefly discussed.

scholarly journals Improved insights into protein thermal stability: from the molecular to the structurome scale

2016 ◽  
Vol 374 (2080) ◽  
pp. 20160141 ◽  
Author(s):  
Fabrizio Pucci ◽  
Marianne Rooman
Keyword(s):  
Thermal Stability ◽  
Amino Acid ◽  
Protein Stability ◽  
Large Scale ◽  
Molecular Level ◽  
Multiscale Approach ◽  
Temperature Dependent ◽  
Natural Evolution ◽  
Large Scale Analysis ◽  
Thermal Stability Of

Despite the intense efforts of the last decades to understand the thermal stability of proteins, the mechanisms responsible for its modulation still remain debated. In this investigation, we tackle this issue by showing how a multiscale perspective can yield new insights. With the help of temperature-dependent statistical potentials, we analysed some amino acid interactions at the molecular level, which are suggested to be relevant for the enhancement of thermal resistance. We then investigated the thermal stability at the protein level by quantifying its modification upon amino acid substitutions. Finally, a large scale analysis of protein stability—at the structurome level—contributed to the clarification of the relation between stability and natural evolution, thereby showing that the mutational profile of proteins differs according to their thermal properties. Some considerations on how the multiscale approach could help in unravelling the protein stability mechanisms are briefly discussed. This article is part of the themed issue ‘Multiscale modelling at the physics–chemistry–biology interface’.

Molecular-Level Insights into Orientation-Dependent Changes in the Thermal Stability of Enzymes Covalently Immobilized on Surfaces

Langmuir ◽  
2015 ◽  
Vol 31 (22) ◽  
pp. 6145-6153 ◽  
Author(s):  
Tadeusz L. Ogorzalek ◽  
Shuai Wei ◽  
Yuwei Liu ◽  
Quiming Wang ◽  
Charles L. Brooks ◽  
...  
Keyword(s):  
Thermal Stability ◽  
Molecular Level ◽  
Thermal Stability Of

scholarly journals Bio-Based Thermo-Reversible Aliphatic Polycarbonate Network

Molecules ◽  
2019 ◽  
Vol 25 (1) ◽  
pp. 74 ◽  
Author(s):  
Pierre-Luc Durand ◽  
Etienne Grau ◽  
Henri Cramail
Keyword(s):  
Thermal Stability ◽  
Biomedical Applications ◽  
Diels Alder ◽  
Cross Linking ◽  
Important Class ◽  
Aliphatic Polycarbonate ◽  
Biomedical Field ◽  
The Cross ◽  
Thermal Stability Of

Aliphatic polycarbonates represent an important class of materials with notable applications in the biomedical field. In this work, low Tg furan-functionalized bio-based aliphatic polycarbonates were cross-linked thanks to the Diels–Alder (DA) reaction with a bis-maleimide as the cross-linking agent. The thermo-reversible DA reaction allowed for the preparation of reversible cross-linked polycarbonate materials with tuneable properties as a function of the pendent furan content that was grafted on the polycarbonate backbone. The possibility to decrosslink the network around 70 °C could be an advantage for biomedical applications, despite the rather poor thermal stability of the furan-functionalized cross-linked polycarbonates.

scholarly journals The influence of stereochemistry on the reactivity of the Diels–Alder cycloaddition and the implications for reversible network polymerization

2019 ◽  
Vol 10 (4) ◽  
pp. 473-485 ◽  
Author(s):  
Audrey Cuvellier ◽  
Robrecht Verhelle ◽  
Joost Brancart ◽  
Bram Vanderborght ◽  
Guy Van Assche ◽  
...  
Keyword(s):  
Thermal Stability ◽  
Thermal Properties ◽  
Polymer Network ◽  
Diels Alder ◽  
Thermal Stability Of

The differences in reactivity and thermal stability of the stereoisomers define the thermal properties and responsiveness of the reversible polymer network.

The use of bisfuroic acid derivatives in the curing of bismaleimides

1994 ◽  
Vol 6 (3) ◽  
pp. 249-256 ◽  
Author(s):  
D G Hawthorne ◽  
J H Hodgkin ◽  
M B Jackson ◽  
T C Morton
Keyword(s):  
Thermal Stability ◽  
Differential Scanning Calorimetry ◽  
Thermal Behaviour ◽  
Thermal Gravimetric Analysis ◽  
Diels Alder ◽  
Gravimetric Analysis ◽  
Resin System ◽  
Thermal Gravimetric ◽  
Scanning Calorimetry ◽  
Thermal Stability Of

The use of 2,2-bis(4-[(2-carboxy-5-furyl)oxy]phenyl)propane as a Diels-Alder based co-reactant for curing bismaleimides was investigated. Differential scanning calorimetry and thermal gravimetric analysis were used to study the thermal behaviour of this reactant on its own and in the presence of 1,1'-(4methylene-4,1-phenylene)bismaleimide. The range of products formed under different cure conditions was determined by vFnR spectroscopy. The DMTA characteristics and thermal stability of cured laminates made from this resin system have been investigated. It is concluded that the thermal stability and other properties of laminates made from this system are only comparable to those of a typical commercial bismaleimide system.

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