A Hierarchical Coarse-Grained (All-Atom-to-All-Residue) Computer Simulation Approach: Self-Assembly of Peptides

Authors

Ras B. Pandey, University of Southern MississippiFollow
Zhifeng Kuang, Wright Patterson Air Force BaseFollow
Barry L. Farmer, University of Southern MississippiFollow

Document Type

Article

Publication Date

8-13-2013

Department

Physics and Astronomy

School

Mathematics and Natural Sciences

Abstract

A hierarchical computational approach (all-atom residue to all-residue peptide) is introduced to study self-organizing structures of peptides as a function of temperature. A simulated residue-residue interaction involving all-atom description, analogous to knowledge-based analysis (with different input), is used as an input to a phenomenological coarse-grained interaction for large scales computer simulations. A set of short peptides P1 (¹H ²S ³S ⁴Y ⁵W ⁶Y ⁷A ⁸F ⁹N ¹⁰N ¹¹K ¹²T) is considered as an example to illustrate the utility. We find that peptides assemble rather fast into globular aggregates at low temperatures and disperse as random-coil at high temperatures. The specificity of the mass distribution of the self-assembly depends on the temperature and spatial lengths which are identified from the scaling of the structure factor. Analysis of energy and mobility profiles, gyration radius of peptide, and radial distribution function of the assembly provide insight into the multi-scale (intra- and inter-chain) characteristics. Thermal response of the global assembly with the simulated residue-residue interaction is consistent with that of the knowledge-based analysis despite expected quantitative differences.

Publication Title

PLoS One

Volume

8

Issue

8

Recommended Citation

Pandey, R. B., Kuang, Z., Farmer, B. L. (2013). A Hierarchical Coarse-Grained (All-Atom-to-All-Residue) Computer Simulation Approach: Self-Assembly of Peptides. PLoS One, 8(8).
Available at: https://aquila.usm.edu/fac_pubs/7821