Facile fabrication of robust multilayer films: visible light-triggered chemical cross-linking by the catalysis of a ruthenium(ii) complex

2011 ◽  
Vol 47 (3) ◽  
pp. 929-931 ◽  
Author(s):  
You Yu ◽  
Hui Zhang ◽  
Caihong Zhang ◽  
Shuxun Cui
Keyword(s):  
Visible Light ◽  
Multilayer Films ◽  
Cross Linking ◽  
Facile Fabrication ◽  
Chemical Cross Linking

Internal Composition versus the Mechanical Properties of Polyelectrolyte Multilayer Films: The Influence of Chemical Cross-Linking†

Langmuir ◽  
2009 ◽  
Vol 25 (24) ◽  
pp. 13809-13819 ◽  
Author(s):  
Thomas Boudou ◽  
Thomas Crouzier ◽  
Rachel Auzély-Velty ◽  
Karine Glinel ◽  
Catherine Picart
Keyword(s):  
Mechanical Properties ◽  
Multilayer Films ◽  
Cross Linking ◽  
Polyelectrolyte Multilayer ◽  
Chemical Cross Linking

scholarly journals Improvement of Stability and Cell Adhesion Properties of Polyelectrolyte Multilayer Films by Chemical Cross-Linking

2004 ◽  
Vol 5 (2) ◽  
pp. 284-294 ◽  
Author(s):  
Ludovic Richert ◽  
Fouzia Boulmedais ◽  
Philippe Lavalle ◽  
Jérôme Mutterer ◽  
Emmanuelle Ferreux ◽  
...  
Keyword(s):  
Cell Adhesion ◽  
Multilayer Films ◽  
Cross Linking ◽  
Polyelectrolyte Multilayer ◽  
Adhesion Properties ◽  
Chemical Cross Linking

Statistical Force-Field for Structural Modeling Using Chemical Cross-Linking/mass Spectrometry Distance Constraints

2018 ◽  
Author(s):  
Allan J. R. Ferrari ◽  
Fabio C. Gozzo ◽  
Leandro Martinez
Keyword(s):  
Mass Spectrometry ◽  
Amino Acid ◽  
Force Field ◽  
Protein Structures ◽  
Protein Structure Determination ◽  
Structural Modeling ◽  
Cross Linking ◽  
Amino Acid Residues ◽  
Distance Constraints ◽  
Chemical Cross Linking

<div><p>Chemical cross-linking/Mass Spectrometry (XLMS) is an experimental method to obtain distance constraints between amino acid residues, which can be applied to structural modeling of tertiary and quaternary biomolecular structures. These constraints provide, in principle, only upper limits to the distance between amino acid residues along the surface of the biomolecule. In practice, attempts to use of XLMS constraints for tertiary protein structure determination have not been widely successful. This indicates the need of specifically designed strategies for the representation of these constraints within modeling algorithms. Here, a force-field designed to represent XLMS-derived constraints is proposed. The potential energy functions are obtained by computing, in the database of known protein structures, the probability of satisfaction of a topological cross-linking distance as a function of the Euclidean distance between amino acid residues. The force-field can be easily incorporated into current modeling methods and software. In this work, the force-field was implemented within the Rosetta ab initio relax protocol. We show a significant improvement in the quality of the models obtained relative to current strategies for constraint representation. This force-field contributes to the long-desired goal of obtaining the tertiary structures of proteins using XLMS data. Force-field parameters and usage instructions are freely available at http://m3g.iqm.unicamp.br/topolink/xlff <br></p></div><p></p><p></p>

scholarly journals Precipitation Polymerization: Precisely Controlled Microsphere Design via Visible‐Light Cross‐Linking of Functional Prepolymers (Adv. Funct. Mater. 26/2020)

2020 ◽  
Vol 30 (26) ◽  
pp. 2070173
Author(s):  
Jordan P. Hooker ◽  
Florian Feist ◽  
Laura Delafresnaye ◽  
Leonie Barner ◽  
Christopher Barner‐Kowollik
Keyword(s):  
Visible Light ◽  
Precipitation Polymerization ◽  
Cross Linking

Facile fabrication of a new BiFeWO6/α-AgVO3 composite with efficient visible-light photocatalytic activity for dye-degradation

2019 ◽  
Vol 92 ◽  
pp. 284-293 ◽  
Author(s):  
Raja Arumugam Senthil ◽  
Meng Sun ◽  
Junqing Pan ◽  
Sedahmed Osman ◽  
Abrar Khan ◽  
...  
Keyword(s):  
Photocatalytic Activity ◽  
Visible Light ◽  
Dye Degradation ◽  
Visible Light Photocatalytic Activity ◽  
Facile Fabrication ◽  
Visible Light Photocatalytic
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