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Biophys J. 2005 Jul;89(1):506-19. Epub 2005 Apr 29.

Mechanically unfolding the small, topologically simple protein L.

Author information

1
School of Biochemistry and Microbiology, Institute of Molecular Biophysics, Centre for Chemical Dynamics, University of Leeds, Leeds, United Kingdom. brock@bmbaxp.leeds.ac.uk

Abstract

beta-sheet proteins are generally more able to resist mechanical deformation than alpha-helical proteins. Experiments measuring the mechanical resistance of beta-sheet proteins extended by their termini led to the hypothesis that parallel, directly hydrogen-bonded terminal beta-strands provide the greatest mechanical strength. Here we test this hypothesis by measuring the mechanical properties of protein L, a domain with a topology predicted to be mechanically strong, but with no known mechanical function. A pentamer of this small, topologically simple protein is resistant to mechanical deformation over a wide range of extension rates. Molecular dynamics simulations show the energy landscape for protein L is highly restricted for mechanical unfolding and that this protein unfolds by the shearing apart of two structural units in a mechanism similar to that proposed for ubiquitin, which belongs to the same structural class as protein L, but unfolds at a significantly higher force. These data suggest that the mechanism of mechanical unfolding is conserved in proteins within the same fold family and demonstrate that although the topology and presence of a hydrogen-bonded clamp are of central importance in determining mechanical strength, hydrophobic interactions also play an important role in modulating the mechanical resistance of these similar proteins.

PMID:
15863479
PMCID:
PMC1366550
DOI:
10.1529/biophysj.105.061465
[Indexed for MEDLINE]
Free PMC Article

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