Pathways and intermediates in forced unfolding of spectrin repeats

SM Altmann, RG Grünberg, PF Lenne, J Ylänne, A Raae, K Herbert, M Saraste, M Nilges, JKH Hoerber

Research output: Contribution to journalArticle (Academic Journal)peer-review

69 Citations (Scopus)


Spectrin repeats are triple-helical coiled-coil domains found in many proteins that are regularly subjected to mechanical stress. We used atomic force microscopy technique and steered molecular dynamics simulations to study the behavior of a wild-type spectrin repeat and two mutants. The experiments indicate that spectrin repeats can form stable unfolding intermediates when subjected to external forces. In the simulations the unfolding proceeded via a variety of pathways. Stable intermediates were associated to kinking of the central helix close to a proline residue. A mutant stabilizing the central helix showed no intermediates in experiments, in agreement with simulation. Spectrin repeats may thus function as elastic elements, extendable to intermediate states at various lengths.
Translated title of the contributionPathways and intermediates in forced unfolding of spectrin repeats
Original languageEnglish
Pages (from-to)1085 - 1096
Number of pages12
Volume10 (8)
Publication statusPublished - Aug 2002

Bibliographical note

Publisher: Cell Press


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