ࡱ>  U@ bjbj +F3    46 >>>h*D6 )z(i(k(k(k(k(k(k($)RL,(9 """( (%%%" 8 i(%"i(%$%%  %n 0Ls>#%%(D(0)%,$,%6 6 , %<H%Z((6 6 D z%"6 6 zBiomolecular Dynamical Simulation: An Investigation Comparing the Effect of Ewald and Reaction Field Electrostatic Treatments on a Small Peptide. Adair D. Richards* * Molecular Organisation and Assembly in Cells Doctoral Training Centre, ý, Coventry, CV4 7AL, UK. Email: A.D.Richards@warwick.ac.uk Biomolecular dynamical simulations can provide a wealth of useful information on the structural behaviour of peptides. One of the largest approximations used in molecular dynamics simulations is the treatment of long-range electrostatics forces and this study analyses parallel simulations of the five-residue twin-arginine translocase peptide treating long-range electrostatics either with Ewald or reaction field methods. It was found that the simulations produced very similar results although the approach using reaction field equations resulted in a slightly more vibrationally active peptide. For the peptide in question, the choice between Ewald and reaction field electrostatic treatment has no significant effect on the results of the simulation. Introduction Molecular dynamics (MD) simulations provide an atomic-resolution depiction of molecular systems which can elicit valuable information about the structure and function of systems of interest. In biomolecular science we can obtain from MD simulations both physico-chemical properties through statistical sampling of a system in equilibrium and an understanding of pathways and mechanisms of, for example, peptide folding, by following individual particle motions.   Fig. 1 Tat signal peptide, RRQGI, at the beginning (left) and end (right) of simulation under precision Ewald electrostatic treatment. Since 1977 when the first MD simulation of biological interest was published1, interdisciplinary research enveloping chemistry, physics and biology, both theoretical and experimental, has developed with a view to understanding the processes involved with protein and peptide folding. Comparing simulation results with experimental data is essential because the experimental data can be used to validate the simulations and the simulations may help to interpret the experiments correctly or guide future experiments. The simulations are limited however by the necessity for an accurate description of the in vivo situation and the computational power needed to accurately describe the forces and motions involved. There is currently insufficient computational power to provide a complete description of all degrees of freedom for a macroscopic system including quantum-mechanical treatment of all nuclei and electrons for both solute and solvent molecules. In recognition of this, concessions are made in the detail of description eg. number of degrees of freedom, in the length of time simulated, the system size and the accuracy of the relevant forces. Even with a reduced set of explicitly treated degrees of freedom, it is computationally impossible to simulate a system large enough to avoid surface effects at the boundary of the box with a vacuum or a dielectric continuum representing the mean effect of solvent outside the system2. This boundary is eliminated by infinitely replicating periodically the system box although this introduces a crystalline order which can lead to periodicity-induced artefacts. Given this periodic microscopic system set-up, an appropriate algorithm is required to treat the pairwise non-bonded interactions, the number of which grows with N2, where N is the number of particles in the system. These can be divided into the Van der Waals interactions which decay rapidly with distance and are generally truncated after an appropriate cut off distance to avoid interactions with more than one periodic copy of other atoms, and the long-range electrostatic forces. There are two approaches to treating the long-range electrostatic interactions and both include severe approximations which may lead to unreliable simulations in some cases.   Fig. 2 Tat signal peptide, RRQGI, at the beginning (left) and end (right) of simulation under reaction field electrostatic treatment with the peptide backbone highlighted in blue. The first approach truncates the Coulombic interactions beyond a cut-off distance using a reaction field (r.f.) method to approximate the mean effect of the outside medium. The other method utilises the exact periodicity of the system and includes all periodic copies of all electrostatic interactions using lattice-sum techniques based upon Ewald summation. A third option, currently in its infancy is the use of continuum electrostatics to permit a systematic analysis or cut-off linked finite-size effects, although this approach ignores the discrete nature of the solvent.  Fig. 3 Ramachandran snapshot plot of an Ewald simulation of the Tat signal peptide. In the reaction field method, each charge is considered individually as the origin of a particular spherical coordinate system. Surrounding it is a cut-off sphere containing explicit neighbouring particles, which itself is placed within a homogeneous dielectric continuum of permittivity matching that of the solvent. Continuum electrostatic equations are then solved using spherical symmetry to estimate the reaction-field force from the continuum onto the particle. This long-range correction is then added to the short-range contribution which is computed via explicit summation over the neighbouring atoms within the cut-off sphere3. As with the reaction-field method, the Ewald approximation methods rely on splitting particle interactions into a short-range component which is computed by pairwise particle-particle summation, and a long-range component computed here by evaluating Fourier series directly. This is based on the assumption of exact periodicity within the simulated system. Previous investigations have questioned the application of artificial periodicity in biomolecular simulations4, suggesting that it may perturb conformational equilibrium resulting in smaller fluctuations and an artificial stabilisation of the most compact state. The short-range component of non-bonded electrostatic interactions is calculated by explicit particle-particle summation with minimum-image spherical truncation. The purpose of this work was to investigate the effect, if any, of applying either a reaction field or Ewald method in simulating a small peptide. The peptide chosen to work with is the five-residue signal peptide involved in the twin-arginine translocase system5. Previous research indicates that the secondary structure of this peptide alternates depending on the hydrophobicity of the environment between helical and unstructured conformations6. Preliminary in-house results indicate a sensitivity in the folding behaviour of the peptide to the way in which the simulations are constructed. The way the long-range electrostatics are treated provides a possible explanation for this. The aim of this study is to establish to what extent the choice between reaction-field and Ewald methods of treating electrostatics affect the behaviour of this small peptide. Experimental procedures An atomistic model of the twin-arginine translocase signal peptide, RRQFI, was set up and energy minimisation calculations were performed in a cubic box of length 20 using the molecular graphics analysis program QUANTA (Accelerys Inc., Cambridge UK) and the CHARMM united atom force field (Vs. 28.1, Accelerys Inc., Cambridge UK) in combination with the DL_POLY7 molecular dynamics package (Vs. 3, CCLLC, Daresbury UK). The peptide was surrounded by 306 molecules (918 atoms) of TIP3P water8 and exported and converted to DL_POLY format using in-house software. The Berendson9 ensemble was chosen to ensure constant pressure at 30 atmospheres and constant temperature at 310K throughout the simulations. For the non-bonded interactions a twin-range method of calculation with cut-off radii of 9 and a Verlet neighbour-list width of 0.5 were used. The long-range electrostatics were either treated using the reaction field method or a precision Ewald method explicitly solving all appropriate Fourier series. Bond lengths were constrained using the SHAKE algorithm10 to a geometric tolerance of 10-4. The simulation ran using a single timestep of 1fs were equilibrated for 5.5ns and then run for 5ns with the trajectory coordinates being recorded every 250fs. The simulations were run using an IBM cluster provided by the Centre for Scientific Computing of the ý with support from Joint Research Equipment Initiative grant JR00WASTEQ. In-house software was then used to reconstruct the output files to avoid abnormal bonds across the box boundary and to convert the files to a VMD compatible format. The molecular visualisation program VMD (CBG, University of Illinois USA) was then used in conjunction with Excel (Microsoft, Redmond USA) to analyse and compare the output files. In addition to this, some secondary structural analysis was conducted using DSSPcont11 (CUBIC, New York USA). Results Figures 1 and 2 are snapshots taken at the beginning and end of the simulations using each electrostatic treatment method and visualised in VMD. The residues are colour coded for ease of recognition. Figure 3 shows a Ramachandran plot of the peptide under an Ewald simulation with the three interior residues represented by dots in the upper-left quadrant and the outer resides represented by dots on the x and y axes. Figures 4 and 5 demonstrate the inter-atomic distance between two carbon molecules in residues 1 and 5 over the 20 000 timesteps and Figures 6 and 7 display similar information regarding two carbons in residues 2 and 4.  Fig. 4 Chart comparing the distance between two carbon atoms on residues 1 and 5 over time under an Ewald electrostatic treatment. Discussion and Conclusion The theoretical backgrounds of reaction field and Ewald electrostatics are very different, with the Ewald methods relying on the precise calculation of electrostatic interactions in an infinite periodic system constructed by making replicas of the unit box, and the reaction field method relying on the truncating of Coulombic interactions within the periodic system and treating the medium outside the cut off sphere of each atom as a dielectric continuum with the same permittivity as the solvent. It would be reasonable to expect that structural and energetic properties obtained from MD simulations will differ as a result of these dissimilar models. It is accepted that Ewald methods in general evaluate the electrostatic interactions more accurately than reaction field methods, giving a slightly lower electrostatic energy than the reaction field12. This results in an expectation that there will be more structural flexibility in reaction field simulations leading to a greater amount of peptide backbone movement over time13.  Fig. 6 Chart comparing the distance between two carbon atoms on residues 2 and 4 over time under a reaction field electrostatic treatment. A visualisation of the degree of structural change experienced over 5ns is displayed (Figures 1 and 2) and there is little change evident to the naked eye. The five residue peptide is too small to use secondary structure prediction and analysis programs such as Stride and DSSPcont effectively. When DSSPcont was applied, it indicated a turn structure for both simulations but the size of error due to the small number of atoms involved renders the result unreliable. Ramachandran plots (snapshot given in Figure 3), predict a combination of a -sheet and unstructured regions in the peptide but again the large error due to the size of the molecule invalidates that conclusion.  Fig. 5 Chart comparing the distance between two carbon atoms on residues 1 and 5 over time under a reaction field electrostatic treatment.  Fig. 7 Chart comparing the distance between two carbon atoms on residues 2 and 4 over time under an Ewald electrostatic treatment. Figures 4 and 5 display a more useful reflection of the peptides vibrations and movement over the 5ns simulation time. With an average distance of 13.37 and 13.00 and standard deviation of 0.199 and 0.247 for the Ewald and reaction field experiments respectively, the peptides conformation undergoes small fluctuations. Evident from the displayed graphs and the standard deviations, there is meaningfully greater structural change experienced under the reaction field method in line with expectations, although this difference is small. Figures 6 and 7 compare the distance between a residue 2 carbon and a residue 4 carbon and provide results in line with those derived from Figures 4 and 5. The evidence from Figures 6 and 7 add weight to the conclusions drawn above and help to eliminate the possibility of the two chosen atoms in Figures 4 and 5 being an anomalous pair. An advantage of MD simulations over Monte Carlo simulations is that each successive iteration of the system is connected to the previous states of the system, which allows us to consider a property of the system, in this case inter-atom distances, as a function of time. Thus we can produce a time correlation coefficient as a measure of correlation between the Ewald and reaction field simulations over time. The normalised version of the time correlation coefficient is given below in equation 1 where x and y represent the inter-atomic distance, i represents the index covering each timestep and M represents the total number of timesteps (20,000). This correlation coefficient was calculated to be 0.9997 in relation to the Ewald and reaction field simulations for inter-atomic distances between residue 1 and residue 5. This is a high correlation, (the maximum correlation is one), and indicates that the simulations produce very similar results. Therefore it can be said that the choice of long-range electrostatic treatment between precision Ewald and reaction field methods has no significant bearing on the outcome of simulations. Future investigations into this area may include conducting longer simulations to establish the existence, if any, of artificial artefacts and dynamics with long time periods. Additionally, MD simulations could be run using a larger peptide to aid data analysis and counter-ions added to the solvent to provide a more realistic ionic environment. A third type of electrostatic treatment could also be considered, namely one of the popular particle-particle particle-mesh Ewald methods such as P3ME/RESPA214. In conclusion, it appears that there is no major difference between using Ewald or reaction field methods for simulating small peptides. There is slightly more peptide flexibility whilst using the reaction field methods as they lead to higher electrostatic energy values in comparison to Ewald simulations. There is currently insufficient evidence to rule out the possibility that different electrostatic treatments will have a significant effect on larger or charge-neutral systems. For the system in question in this study however, any effect due to the choice of electrostatic interactions is negligible. Acknowledgements The author would like to thank the following for their guidance and help: Mark Rodger and Rob Hawtin at the ý, Syma Khalid at Oxford University, Philip Carter at Imperial College London and Miguel San Miguel at Universidad de Sevilla. This work was funded by the Experimental and Physical Sciences Research Council Life Sciences Initiative. References 1 McCammon, J.A., Gelin, B.R. & Karplus, M. (1977). Dynamics of folded proteins. Nature, 267, 585-590. 2 Bergdorf, P., (2003). Influence of cutoff truncation and artificial periodicity in electrostatic interactions of molecular dynamics simulations of solvated ions: a continuum dielectrics study. Submitted to J. Chem.. Phys. 3 Peter, C., (2003) A critical analysis of various aspects of biomolecular simulation: from electrostatic forces, NMR spectra and entropy to peptide folding. Thesis 15160, Shaker Verlag: Zurich. 4 Kastenholz, M.A. & Hunenberger, P.H., (2004). Influence of artificial periodicity and ionic strength in molecular dynamics simulations of charged biomolecules employing lattice-sum methods. J. Phys. Chem. B, 108, 774-788. 5 Robinson, C. & Bolhuis, A. (2001). Protein targeting by the twin-arginine translocation pathway. Nat. Rev. Mol. Cell. Biol., 2, 350-355. 6 San Miguel, M. et al., (2003). An Escherichia coli twin-arginine signal peptide switches between helical and unstructured conformations depending on the hydrophobicity of the environment. Eur. J. Biochem., 270, 3345-3352. 7 Smith, W., Yong, C.W. & Rodger, P.M., (2002). DL_POLY: application to molecular simulation. Mol. Sim., 28, 385-471. 8 Jorgensen, W.L. et al., (1983). Comparison of simple potential functions for simulating liquid water. J. Chem. Phys., 79, 926-935. 9 Berendsen, H.J.C. et al., (1984). Molecular dynamics with coupling to an external bath. J. Chem. Phys., 81(8), 3684-3690., 10 Brooks, B.R. et al. (1983). A program for macromolecular energy, minimization, and dynamics calculations. J. Comp. Chem., 4, 187-217. 11 Anderson, C.A.F. et al., (2002). Continuum secondary structure captures protein flexibility. Structure, 10, 175-185. 12 Ryckaert, J.P., Ciccotti, G. & Berendsen, H.J.C. (1977). Numerical integration of the Cartesian equation of integration of motion of a system with constraints: molecular dynamics of N-alkanes. J. Comp. Phys., 23, 327. 13 Gargallo, R. et al., (2003). Molecular dynamics simulation of highly charged proteins: Comparison of the particle-particle particle-mesh and reaction field methods for the calculation of electrostatic interactions. Prot. Sci., 12, 2161-2172. 14 Zhou, R. et al., (2001). Efficient multiple time step method for use with Ewald and particle mesh Ewald for large biomolecular systems. J. Chem. Phys., 115(5), 2348-2358.  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