Mechanical Unfoldons as Building Blocks of Maltose-binding Protein

Morten Bertz, Matthias Rief*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

63 Citations (Scopus)


Identifying independently folding cores or substructures is important for understanding and assaying the structure, function and assembly of large proteins. Here, we suggest mechanical stability as a criterion to identify building blocks of the 366 amino acid maltose-binding protein (MBP). We find that MBP, when pulled at its termini, unfolds via three (meta-) stable unfolding intermediates. Consequently, the MBP structure consists of four structural blocks (unfoldons) that detach sequentially from the folded structure upon force application. We used cysteine cross-link mutations to characterize the four unfoldons structurally. We showed that many MBP constructs composed of those building blocks indeed form stably folded structures in solution. Mechanical unfoldons may provide a new tool for a systematic search for stable substructures of large proteins.

Original languageEnglish
Pages (from-to)447-458
Number of pages12
JournalJournal of Molecular Biology
Issue number2
Publication statusPublished - 2008 Apr 25
Externally publishedYes


  • atomic force microscopy
  • energy landscape
  • protein folding
  • single-molecule force spectroscopy
  • unfolding intermediate

ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology


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