Mechanical unfolding of ubiquitin molecules

Mechanical stretching of ubiquitin and of its several repeats are studied through molecular-dynamics simulations. A Go-type model [H. Abe and N. Go, Biopolymers 20, 1013 (1981)] with a realistic contact map and with Lennard-Jones contact interactions is used. The model qualitatively reproduces the experimentally observed differences between force-extension patterns obtained on polyubiquitins stretched by various linkages. The terminal-to-terminal stretching of polyubiquitin results in peak forces similar to those measured for titin-based polyproteins and of a magnitude that matches measurements. Consistent with the experimental measurements, the simulated peak forces depend on the pulling speed logarithmically when thermal fluctuations are explicitly introduced. These results validate the application of topology-based models in the study of the mechanical stretching of proteins. © 2005 American Institute of Physics.

Full Text

Duke Authors

Cited Authors

  • Cieplak, M; Marszalek, PE

Published Date

  • 2005

Published In

Volume / Issue

  • 123 / 19

International Standard Serial Number (ISSN)

  • 0021-9606

Digital Object Identifier (DOI)

  • 10.1063/1.2046609

Citation Source

  • SciVal