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Unfolding forces of titin and fibronectin domains directly measured by AFM

  • M. Rief
  • , M. Gautel
  • , H. E. Gaub
  • , Pollack
  • , Vigoreaux
  • , Qian
  • , TerKeurs
  • , Trombitás
  • , Granzier
  • , Linke
  • , Sanger
  • Stanford University School of Medicine

Research output: Contribution to journalArticlepeer-review

78 Scopus citations

Abstract

AFM-based Single Molecule Force Spectroscopy provides a new tool for probing the mechanical properties of single molecules. In this chapter we show that the unfolding forces of single protein domains can be directly measured. Unfolding forces give new insight into protein stability that cannot be deduced from thermodynamic measurements. A comparison between the unfolding forces measured in Ig domains of the muscle protein titin and those measured in fibronectin Type III domains reveals an extraordinarily high stability of titin domains.

Original languageEnglish
Pages (from-to)129-141
Number of pages13
JournalAdvances in Experimental Medicine and Biology
Volume481
DOIs
StatePublished - 2000
Externally publishedYes

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