Routine Access to Millisecond Time Scale Events with Accelerated Molecular Dynamics
Author(s) -
Levi Pierce,
Romelia Salomón–Ferrer,
César Augusto F. de Oliveira,
J. Andrew McCammon,
Ross C. Walker
Publication year - 2012
Publication title -
journal of chemical theory and computation
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.001
H-Index - 185
eISSN - 1549-9626
pISSN - 1549-9618
DOI - 10.1021/ct300284c
Subject(s) - millisecond , computer science , molecular dynamics , suite , sampling (signal processing) , computational science , software , graphics , scale (ratio) , chemistry , computational chemistry , physics , computer graphics (images) , operating system , archaeology , filter (signal processing) , quantum mechanics , astronomy , computer vision , history
In this work, we critically assess the ability of the all-atom enhanced sampling method accelerated molecular dynamics (aMD) to investigate conformational changes in proteins that typically occur on the millisecond time scale. We combine aMD with the inherent power of graphics processor units (GPUs) and apply the implementation to the bovine pancreatic trypsin inhibitor (BPTI). A 500 ns aMD simulation is compared to a previous millisecond unbiased brute force MD simulation carried out on BPTI, showing that the same conformational space is sampled by both approaches. To our knowledge, this represents the first implementation of aMD on GPUs and also the longest aMD simulation of a biomolecule run to date. Our implementation is available to the community in the latest release of the Amber software suite (v12), providing routine access to millisecond events sampled from dynamics simulations using off the shelf hardware.
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