Nature Structural Biology10, 731 - 737 (2003)
Published online: 17 August 2003; | doi:10.1038/nsb968
There is an Erratum (October 2003) associated with this Article.
Pulling geometry defines the mechanical resistance of a -sheet
protein
David J Brockwell1, Emanuele Paci2, Rebecca C Zinober1, 3, Godfrey S Beddard4, Peter D Olmsted3, D Alastair Smith3, Richard N Perham5
& Sheena E Radford1
1
School of Biochemistry and Molecular Biology,
University of Leeds, LS2 9JT, UK.
Proteins show diverse responses when placed under mechanical
stress. The molecular origins of their differing mechanical resistance are
still unclear, although the orientation of secondary structural elements
relative to the applied force vector is thought to have an important function.
Here, by using a method of protein immobilization that allows force to be
applied to the same all- protein, E2lip3, in two different directions, we
show that the energy landscape for mechanical unfolding is markedly
anisotropic. These results, in combination with molecular dynamics (MD)
simulations, reveal that the unfolding pathway depends on the pulling geometry
and is associated with unfolding forces that differ by an order of magnitude.
Thus, the mechanical resistance of a protein is not dictated solely by amino
acid sequence, topology or unfolding rate constant, but depends critically on
the direction of the applied extension.
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-sheet
protein
protein, E2lip3, in two different directions, we
show that the energy landscape for mechanical unfolding is markedly
anisotropic. These results, in combination with molecular dynamics (MD)
simulations, reveal that the unfolding pathway depends on the pulling geometry
and is associated with unfolding forces that differ by an order of magnitude.
Thus, the mechanical resistance of a protein is not dictated solely by amino
acid sequence, topology or unfolding rate constant, but depends critically on
the direction of the applied extension.
