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The mechanical stability of ubiquitin is linkage dependent.

Publication ,  Journal Article
Carrion-Vazquez, M; Li, H; Lu, H; Marszalek, PE; Oberhauser, AF; Fernandez, JM
Published in: Nature structural biology
September 2003

Ubiquitin chains are formed through the action of a set of enzymes that covalently link ubiquitin either through peptide bonds or through isopeptide bonds between their C terminus and any of four lysine residues. These naturally occurring polyproteins allow one to study the mechanical stability of a protein, when force is applied through different linkages. Here we used single-molecule force spectroscopy techniques to examine the mechanical stability of N-C-linked and Lys48-C-linked ubiquitin chains. We combined these experiments with steered molecular dynamics (SMD) simulations and found that the mechanical stability and unfolding pathway of ubiquitin strongly depend on the linkage through which the mechanical force is applied to the protein. Hence, a protein that is otherwise very stable may be easily unfolded by a relatively weak mechanical force applied through the right linkage. This may be a widespread mechanism in biological systems.

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Published In

Nature structural biology

DOI

ISSN

1072-8368

Publication Date

September 2003

Volume

10

Issue

9

Start / End Page

738 / 743

Related Subject Headings

  • Ubiquitin
  • Protein Structure, Tertiary
  • Protein Folding
  • Protein Binding
  • Polyubiquitin
  • Models, Molecular
  • Microscopy, Atomic Force
  • Lysine
  • Kinetics
  • Hydrogen Bonding
 

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Carrion-Vazquez, M., Li, H., Lu, H., Marszalek, P. E., Oberhauser, A. F., & Fernandez, J. M. (2003). The mechanical stability of ubiquitin is linkage dependent. Nature Structural Biology, 10(9), 738–743. https://doi.org/10.1038/nsb965
Carrion-Vazquez, Mariano, Hongbin Li, Hui Lu, Piotr E. Marszalek, Andres F. Oberhauser, and Julio M. Fernandez. “The mechanical stability of ubiquitin is linkage dependent.Nature Structural Biology 10, no. 9 (September 2003): 738–43. https://doi.org/10.1038/nsb965.
Carrion-Vazquez M, Li H, Lu H, Marszalek PE, Oberhauser AF, Fernandez JM. The mechanical stability of ubiquitin is linkage dependent. Nature structural biology. 2003 Sep;10(9):738–43.
Carrion-Vazquez, Mariano, et al. “The mechanical stability of ubiquitin is linkage dependent.Nature Structural Biology, vol. 10, no. 9, Sept. 2003, pp. 738–43. Epmc, doi:10.1038/nsb965.
Carrion-Vazquez M, Li H, Lu H, Marszalek PE, Oberhauser AF, Fernandez JM. The mechanical stability of ubiquitin is linkage dependent. Nature structural biology. 2003 Sep;10(9):738–743.

Published In

Nature structural biology

DOI

ISSN

1072-8368

Publication Date

September 2003

Volume

10

Issue

9

Start / End Page

738 / 743

Related Subject Headings

  • Ubiquitin
  • Protein Structure, Tertiary
  • Protein Folding
  • Protein Binding
  • Polyubiquitin
  • Models, Molecular
  • Microscopy, Atomic Force
  • Lysine
  • Kinetics
  • Hydrogen Bonding