Spectroscopic Study on the Structural Differences of Thermally Induced Cross-Linking Segments in Emeraldine Salt and Base Forms of Polyaniline

2012 ◽  
Vol 116 (48) ◽  
pp. 14191-14200 ◽  
Author(s):  
Marcelo M. Nobrega ◽  
Claudio H. B. Silva ◽  
Vera R. L. Constantino ◽  
Marcia L. A. Temperini
Keyword(s):  
Spectroscopic Study ◽  
Cross Linking ◽  
Emeraldine Salt ◽  
Thermally Induced ◽  
Structural Differences

Thermally induced chemical cross-linking reinforced fluorinated polyurethane/polyacrylonitrile/polyvinyl butyral nanofibers for waterproof-breathable application

RSC Advances ◽  
2016 ◽  
Vol 6 (35) ◽  
pp. 29629-29637 ◽  
Author(s):  
Junlu Sheng ◽  
Min Zhang ◽  
Wenjing Luo ◽  
Jianyong Yu ◽  
Bin Ding
Keyword(s):  
Polyvinyl Butyral ◽  
Cross Linking ◽  
Thermally Induced ◽  
Fluorinated Polyurethane ◽  
Nanofibrous Membranes ◽  
Chemical Cross Linking

Thermally induced chemical cross-linking could enhance the FPAN/PVB/BIP composite nanofibrous membranes with robust mechanical, waterproof and breathable performance.

scholarly journals Optimized structure of monoubiquitinated FANCD2 (human) at Lys 561: a theoretical approach

2021 ◽  
Author(s):  
Sudipa Mondal ◽  
Subba Reddy ◽  
Sudit S. Mukhopadhyay
Keyword(s):  
Crystal Structure ◽  
Molecular Dynamics ◽  
Theoretical Approach ◽  
Md Simulation ◽  
Docking Studies ◽  
Fanconi Anaemia ◽  
Cross Linking ◽  
Structural Differences ◽  
The Stability ◽  
Dna Docking

AbstractFanconi anaemia pathway repairs inter-strand cross linking damage (ICL) of the DNA. Monoubiquitination of FANCD2 and FANCI is very crucial for ICL repairing. In this work we have tried to understand the monoubiquitinated FANCD2 structure, which facilitates the FANCD2 for binding the damage part of the chromatin. Crystal structure of the monoubiquitinated FANCD2 alone is not available, therefore we have developed the optimized structure of the human monoubiquitinated (Lys 561) FANCD2. As there is no suitable software or web server we have developed a method for building up monoubiquitinated product and validated on simplest monoubiquitinated protein, diubiquitin. We have predicted the structure of human monoubiquitinated FANCD2 by using our method and studied the interaction with DNA by docking studies. Molecular Dynamics (MD) simulation was used to understand the stability of the structure. Large structural differences have been observed between FANCD2 and monoubiquitinated FANCD2. DNA docking studies suggest that the binding site varies for the FANCD2 and monoubiquitinated FANCD2.

scholarly journals Structure of complement C3(H2O) revealed by quantitative cross-linking/mass spectrometry and modeling

2016 ◽  
Author(s):  
Zhuo A. Chen ◽  
Riccardo Pellarin ◽  
Lutz Fischer ◽  
Andrej Sali ◽  
Michael Nilges ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
3D Model ◽  
Domain Architecture ◽  
Factor H ◽  
Complement C3 ◽  
Cross Linking ◽  
First Line ◽  
Structural Differences ◽  
The Complement System

AbstractThe slow but spontaneous and ubiquitous formation of C3(H2O), the hydrolytic and conformationally rearranged product of C3, initiates antibody-independent activation of the complement system that is a key first line of antimicrobial defense. The structure of C3(H2O) has not been determined. Here we subjected C3(H2O) to quantitative cross-linking/mass spectrometry (QCLMS). This revealed details of the structural differences and similarities between C3(H2O) and C3, as well as between C3(H2O) and its pivotal proteolytic cleavage product, C3b, which shares functionally similarity with C3(H2O). Considered in combination with the crystal structures of C3 and C3b, the QCMLS data suggest that C3(H2O) generation is accompanied by the migration of the thioester-containing domain of C3 from one end of the molecule to the other. This creates a stable C3b-like platform able to bind the zymogen, factor B, or the regulator, factor H. Integration of available crystallographic and QCLMS data allowed the determination of a 3D model of the C3(H2O) domain architecture. The unique arrangement of domains thus observed in C3(H2O), which retains the anaphylatoxin domain (that is excised when C3 is enzymatically activated to C3b), can be used to rationalize observed differences between C3(H2O) and C3b in terms of complement activation and regulation.

Thermally Induced Cross-Linking and Degradation Reactions of Benzocyclobutene-Based Polymers

2017 ◽  
Vol 50 (6) ◽  
pp. 2304-2319 ◽  
Author(s):  
Anthony P. Gies ◽  
Liam Spencer ◽  
Nathan J. Rau ◽  
Praveenkumar Boopalachandran ◽  
Mark A. Rickard ◽  
...  
Keyword(s):  
Cross Linking ◽  
Thermally Induced ◽  
Degradation Reactions

scholarly journals Diazo-Based Copolymers for the Wet Strength Improvement of Paper Based on Thermally Induced CH-Insertion Cross-Linking

2021 ◽  
Author(s):  
Simon Schölch ◽  
Jan-Lukas Schäfer ◽  
Tobias Meckel ◽  
Thomas Brandstetter ◽  
Markus Biesalski ◽  
...  
Keyword(s):  
Cross Linking ◽  
Wet Strength ◽  
Thermally Induced ◽  
Strength Improvement
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