Leveraging symmetry to predict self-assembly of multiple polymers

Research output: Contribution to journalArticle

1 Scopus citations

Abstract

Protein self-assembly is fundamental to biological function and disease. Experimentally, the atomic-level structure is difficult to obtain and the assembly mechanism is poorly understood. The large number of possible states accessible to such systems limits computational prediction. Here, I introduce a new computational approach that enforces conformational symmetry, whereby all chains in the system adopt the same conformation. Using this approach on a 2D lattice, a designed multi-chain conformation is found more than four orders of magnitude faster than existing approaches. Furthermore, the free energy landscape can be efficiently computed, showing potential for enabling atomistic prediction of protein self-assembly.

Original languageEnglish (US)
Pages (from-to)347-351
Number of pages5
JournalChemical Physics Letters
Volume683
DOIs
StatePublished - Sep 1 2017

ASJC Scopus subject areas

  • Physics and Astronomy(all)
  • Physical and Theoretical Chemistry

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