Mussel Glue Protein Has an Open Conformation

Abstract

Most of the cells and tissues of living organisms rely on a very specific and dynamic array of molecular interactions for their cohesive integrity. In contrast, the attachment of marine mussels to a variety of surfaces ranging from paraffin to slate is remarkable for its nonspecificity and permanence. The polyphenolic or glue protein responsible for mussel adhesion has recently been characterized. The protein adsorbs to surfaces following secretion as a semistable foam by foot of the mussel. Subsequently, the foam hardens and forms a permanent bond between the surface and the mostly collagenous byssal threads. Circular dichroism and enzymatic modification studies suggest that the mussel glue protein may have a largely unordered extended conformation in solution with little or no secondary structure. Keywords: Reprints; Adhesives.

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Document Details

Document Type
Technical Report
Publication Date
Mar 01, 1989
Accession Number
ADA208148

Entities

People

  • J. H. Waite
  • Keishi Marumo
  • Robert W. Henkens
  • Taffy Williams

Organizations

  • Naval Medical Research Center

Tags

Communities of Interest

  • Biomedical

DTIC Thesaurus Topics

  • Adhesion
  • Adhesives
  • Amino Acids
  • Biochemistry
  • Biomedical Research
  • Cells
  • Chemical Compounds
  • Chemical Synthesis
  • Chemistry
  • Classification
  • Dichroism
  • Elements
  • Fungi
  • Materials
  • Mixing
  • Probability
  • Vitamin C

Readers

  • Distributed Systems and Data Platform Development
  • Molecular and Cellular Biochemistry
  • Surface Coatings Technology.