28559 articles – 22057 references  [version française]

inria-00390312, version 1

Adaptive torsion-angle quasi-statics: a general simulation method with applications to protein structure analysis and design

Romain Rossi 1, Mathieu Isorce 23, Sandy Morin 1, Julien Flocard 23, Karthik Arumugam 23, Serge Crouzy 23, Michel Vivaudou 3, Stephane Redon (Author to contact preferably) a1

Bioinformatics (2007)

Abstract: Motivation: The cost of molecular quasi-statics or dynamics simulations increases with the size of the simulated systems, which is a problem when studying biological phenomena that involve large molecules over long time scales. To address this problem, one has often to either increase the processing power (which might be expensive), or make arbitrary simplifications to the system (which might bias the study). Results: We introduce adaptive torsion-angle quasi-statics, a general simulation method able to rigorously and automatically predict the most mobile regions in a simulated system, under user-defined precision or time constraints. By predicting and simulating only these most important regions, the adaptive method provides the user with complete control on the balance between precision and computational cost, without requiring him or her to perform a priori, arbitrary simplifications. We build on our previous research on adaptive articulated-body simulation and show how, by taking advantage of the partial rigidification of a molecule, we are able to propose novel data structures and algorithms for adaptive update of molecular forces and energies. This results in a globally adaptive molecular quasi-statics simulation method. We demonstrate our approach on several examples and show how adaptive quasi-statics allows a user to interactively design, modify and study potentially complex protein structures.

  • a –  INRIA
  • 1:  I3D (INRIA Grenoble Rhône-Alpes / LIG Laboratoire d'Informatique de Grenoble)
  • INRIA – Institut polytechnique de Grenoble (Grenoble INP) – Université Joseph Fourier - Grenoble I – Université Pierre-Mendès-France - Grenoble II – CNRS : UMR5217
  • 2:  Laboratoire de Chimie et Biologie des Métaux (LCBM)
  • CNRS : UMR5249 – CEA : DSV/IRTSV – Université Joseph Fourier - Grenoble I
  • 3:  Laboratoire de biophysique moléculaire et cellulaire (LBMC)
  • CNRS : UMR5090 – CEA : DSV/IRTSV – Université Joseph Fourier - Grenoble I
  • Domain : Computer Science/Modeling and Simulation
 
  • inria-00390312, version 1
  • oai:hal.inria.fr:inria-00390312
  • From: 
  • Submitted on: Monday, 1 June 2009 18:34:11
  • Updated on: Friday, 12 June 2009 11:33:54