Molecular models to emulate confinement effects on the internal dynamics of organophosphorous hydrolase

Diego E.B. Gomes, Roberto D. Lins, Pedro G. Pascutti, Tjerk P. Straatsma, Thereza A. Soares

Research output: Chapter in Book/Report/Conference proceedingConference contributionpeer-review

1 Scopus citations

Abstract

The confinement of the metalloenzyme organophosphorous hydrolase in functionalized mesoporous silica (FMS) enhances the stability and increases catalytic specific activity by 200% compared to the enzyme in solution. The mechanism by which these processes take place is not well understood. We have developed macroscopic and coarse-grain models of confinement to provide insights into how the nanocage environment steers enzyme conformational dynamics towards enhanced stability and enzymatic activity. The structural dynamics of organophosphorous hydrolase under the two confinement models are very distinct from each other. Comparisons of the present simulations show that only one model leads to an accurate depiction of the internal dynamics of the enzyme.

Original languageEnglish
Title of host publicationAdvances in Bioinformatics and Computational Biology - Third Brazilian Symposium on Bioinformatics, BSB 2008, Proceedings
Pages68-78
Number of pages11
DOIs
StatePublished - 2008
Externally publishedYes
Event3rd Brazilian Symposium on Bioinformatics, BSB 2008 - Santo Andre, Brazil
Duration: Aug 28 2008Aug 30 2008

Publication series

NameLecture Notes in Computer Science (including subseries Lecture Notes in Artificial Intelligence and Lecture Notes in Bioinformatics)
Volume5167 LNBI
ISSN (Print)0302-9743
ISSN (Electronic)1611-3349

Conference

Conference3rd Brazilian Symposium on Bioinformatics, BSB 2008
Country/TerritoryBrazil
CitySanto Andre
Period08/28/0808/30/08

Keywords

  • Atomistic molecular dynamics
  • Enhanced catalytic activity
  • Enzyme im-mobilization
  • Functionalized nanoporous support
  • Phosphotriesterase

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