Search for: protein-polymerization
HRP-dendron nanoparticles: The efficient biocatalyst for enzymatic polymerization of poly(2,5-dimethoxyaniline), Article Journal of Molecular Catalysis B: Enzymatic ; Volume 90 , June , 2013 , Pages 139-143 ; 13811177 (ISSN) ; Vossoughi, M ; Shahrokhian, S ; Alemzadeh, I ; Sharif University of Technology
Synthesis of poly(2,5-dimethoxyanilie) (PDMA) catalyzed by nano reengineered horseradish peroxidase (HRP) with dendritic macromolecules, was studied as a function of reaction media. UV-vis, gel permeation chromatography and conductivity measurements were used to explain how the reaction media compositions influence the physical properties of PDMA. Nanostructured PDMA was also synthesized by oxidative polymerization in a novel and green bi-catalyst system involving HRP and ferric chloride. FTIR and UV-vis analysis confirmed the formation of emeraldine salt state of PDMA. The thermal stability of reengineered HRP granted further studies on the polymerization using bi-catalyst system at...
Molecular dynamics simulation and MM-PBSA calculations of sickle cell hemoglobin in dimer form with Val, Trp, or Phe at the lateral contact, Article Journal of Physical Organic Chemistry ; Volume 23, Issue 9 , March , 2010 , Pages 866-877 ; 08943230 (ISSN) ; Akbarzadeh, H ; Parsafar, G. A ; Sharif University of Technology
As the delay time and hence nuclei formation play a crucial role in the pathophysiology of sickle cell disease, MD simulation and molecular mechanics-Poisson-Boltzmann surface area (MM-PBSA) calculations have been performed on three systems of hemoglobin; namely dimer of hemoglobin with valine (Hb S), tryptophan (Hbβ6W), and phenylalanine (Hbβ6F) at β6 position. The structural changes due to these aromatic substitutions are investigated. It is shown that β subunits have significant impact on the differences between a dimer and other crystal structures. Transition from a dimer to polymer for Hb S system affects the donor molecule more than that of the acceptor. In the case of donor and...