Comparing generalized ensemble methods for sampling of systems with many degrees of freedom.

We compare two standard replica exchange methods using temperature and dielectric constant as the scaling variables for independent replicas against two new corresponding enhanced sampling methods based on non-equilibrium statistical cooling (temperature) or descreening (dielectric). We test the four methods on a rough 1D potential as well as for alanine dipeptide in water, for which their relatively small phase space allows for the ability to define quantitative convergence metrics. We show that both dielectric methods are inferior to the temperature enhanced sampling methods, and in turn show that temperature cool walking (TCW) systematically outperforms the standard temperature replica exchange (TREx) method. We extend our comparisons of the TCW and TREx methods to the 5 residue met-enkephalin peptide, in which we evaluate the Kullback-Leibler divergence metric to show that the rate of convergence between two independent trajectories is faster for TCW compared to TREx. Finally we apply the temperature methods to the 42 residue amyloid-β peptide in which we find non-negligible differences in the disordered ensemble using TCW compared to the standard TREx. All four methods have been made available as software through the OpenMM Omnia software consortium (http://www.omnia.md/).

[1]  A. Mark,et al.  Convergence and sampling efficiency in replica exchange simulations of peptide folding in explicit solvent. , 2007, The Journal of chemical physics.

[2]  Daniel R. Roe,et al.  Evaluation of Enhanced Sampling Provided by Accelerated Molecular Dynamics with Hamiltonian Replica Exchange Methods , 2014, The journal of physical chemistry. B.

[3]  K. Sanbonmatsu,et al.  Structure of Met‐enkephalin in explicit aqueous solution using replica exchange molecular dynamics , 2002, Proteins.

[4]  D. Selkoe,et al.  Soluble protein oligomers in neurodegeneration: lessons from the Alzheimer's amyloid β-peptide , 2007, Nature Reviews Molecular Cell Biology.

[5]  D. Wemmer,et al.  Differences in β-strand populations of monomeric Aβ40 and Aβ42. , 2013, Biophysical journal.

[6]  Diwakar Shukla,et al.  OpenMM 4: A Reusable, Extensible, Hardware Independent Library for High Performance Molecular Simulation. , 2013, Journal of chemical theory and computation.

[7]  Hisashi Okumura,et al.  Coulomb replica‐exchange method: Handling electrostatic attractive and repulsive forces for biomolecules , 2013, J. Comput. Chem..

[8]  D. Wemmer,et al.  Comparison of Structure Determination Methods for Intrinsically Disordered Amyloid-β Peptides , 2014, The journal of physical chemistry. B.

[9]  Y. Sugita,et al.  Replica-exchange molecular dynamics method for protein folding , 1999 .

[10]  Nicolas L. Fawzi,et al.  Homogeneous and heterogeneous tertiary structure ensembles of amyloid-β peptides. , 2011, Biochemistry.

[11]  K Schulten,et al.  VMD: visual molecular dynamics. , 1996, Journal of molecular graphics.

[12]  Y. Sugita,et al.  Multidimensional replica-exchange method for free-energy calculations , 2000, cond-mat/0009120.

[13]  Greg L. Hura,et al.  Development of an improved four-site water model for biomolecular simulations: TIP4P-Ew. , 2004, The Journal of chemical physics.

[14]  Jose C. Flores-Canales,et al.  Targeting electrostatic interactions in accelerated molecular dynamics with application to protein partial unfolding. , 2015, Journal of chemical theory and computation.

[15]  W. Nadler,et al.  Optimized explicit-solvent replica exchange molecular dynamics from scratch. , 2008, The journal of physical chemistry. B.

[16]  V. Hornak,et al.  Comparison of multiple Amber force fields and development of improved protein backbone parameters , 2006, Proteins.

[17]  J. Schofield,et al.  Extended state-space Monte Carlo methods. , 2001, Physical review. E, Statistical, nonlinear, and soft matter physics.

[18]  W. L. Jorgensen,et al.  Comparison of simple potential functions for simulating liquid water , 1983 .

[19]  Edward Lyman,et al.  A Second Look at Canonical Sampling of Biomolecules using Replica Exchange Simulation. , 2006, Journal of chemical theory and computation.

[20]  S. Takada,et al.  On the Hamiltonian replica exchange method for efficient sampling of biomolecular systems: Application to protein structure prediction , 2002 .

[21]  U. Hansmann Parallel tempering algorithm for conformational studies of biological molecules , 1997, physics/9710041.

[22]  Scott Brown,et al.  Cool walking: A new Markov chain Monte Carlo sampling method , 2003, J. Comput. Chem..