DNA-protein interactions as the source of large-length-scale chirality evident in the liquid crystal behavior of filamentous bacteriophages

Sonit Tomar, Mark M. Green, Loren A. Day

Research output: Contribution to journalArticlepeer-review

Abstract

Although all filamentous phages are constructed of chiral components, this study of eight of these phages (fd, IKe, I22, X-2, Pf1, Pf3, tf-1, and X) shows that some form nematic liquid crystals, which are apparently oblivious to the chirality of the components, while others form cholesteric liquid crystals revealing a type of structural chirality not normally encountered. Additions of dopants that interact with the DNA or protein components of the viruses change the liquid crystal properties of seven of the phages. In these seven, DNA-capsid symmetry differences do not allow strict structural equivalency among the protein subunits. The polymorphism arising from this nonequivalency is proposed here to give rise to coiling of the filaments, a large-length-scale chirality that is responsible for forming cholesteric liquid crystal phases. Only one phage of those studied here, Pf1, which is distinguished from the others in its DNA-capsid interactions, forms nematic phases under all conditions tried. The formation of liquid crystals has been developed as a method to detect subtle overall shape effects arising from DNA-subunit-derived polymorphism, an unusual role for the mesogenic state and a new tool for the study of filamentous phage structure.

Original languageEnglish (US)
Pages (from-to)3367-3375
Number of pages9
JournalJournal of the American Chemical Society
Volume129
Issue number11
DOIs
StatePublished - Mar 21 2007

ASJC Scopus subject areas

  • Catalysis
  • Chemistry(all)
  • Biochemistry
  • Colloid and Surface Chemistry

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