Slightly Bizarre Protein Chemistry: Urea-Formaldehyde Resin from a Biochemical Perspective

A. Keith Dunker, William E. John, Richard Rammon, Barry Farmer, Susan J. Johns

Research output: Contribution to journalArticle

30 Scopus citations


A linear urea-formaldehyde polymer and a glycine polypeptide have a significant degree of chemical similarity. The low solubility of fibrous proteins, the planarity of the peptide bond, the existence of hydrogen-bonded structures such as a-helices and β-sheets when considered together, suggest new possibilities for interpreting the structure of the urea-formaldehyde polymer. These new possibilities could provide a chemical explanation for urea-formaldehyde solids based on colloidal substructure as has been proposed recently. X-ray diffraction patterns from urea-formaldehyde resins, reported here for the first time, as well as laser Raman spectra, lend support to the proposal that UF resins may contain protein-like colloidal regions of semicrystalline nature.

Original languageEnglish (US)
Pages (from-to)153-176
Number of pages24
JournalThe Journal of Adhesion
Issue number2
StatePublished - Jan 1 1986



  • Alpha-helix
  • Beta-sheet
  • Biochemical perspective
  • Colloidal structure
  • Protein-like structure
  • Urea-formaldehyde polymer

ASJC Scopus subject areas

  • Chemistry(all)
  • Mechanics of Materials
  • Surfaces and Interfaces
  • Surfaces, Coatings and Films
  • Materials Chemistry

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