PH-dependent dimerization and salt-dependent stabilization of the N-terminal domain of spider dragline silk - Implications for fiber formation

Franz Hagn, Christopher Thamm, Thomas Scheibel, Horst Kessler

Research output: Contribution to journalArticlepeer-review

124 Scopus citations

Abstract

One of the toughest protein fibers: The N-terminal domain (NTD) of spider dragline silk shows a pH-dependent monomer-dimer equilibrium: The N-terminal domain silk protein is stored as a stabilized monomer at neutral pH and high salt concentration, whereas during fiber assembly at a lower pH value this domain is able to form antiparallel dimers. Multivalent linking results in endless and highly stable fibers (see picture).

Original languageEnglish
Pages (from-to)310-313
Number of pages4
JournalAngewandte Chemie International Edition in English
Volume50
Issue number1
DOIs
StatePublished - 3 Jan 2011

Keywords

  • NMR spectroscopy
  • biopolymers
  • circular dichroism
  • protein folding
  • protein structure

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