High-speed force spectroscopy unfolds titin at the velocity of molecular dynamics simulations Academic Article uri icon

Overview

MeSH Major

  • Connectin
  • Protein Unfolding
  • Spectrum Analysis

abstract

  • The mechanical unfolding of the muscle protein titin by atomic force microscopy was a landmark in our understanding of single-biomolecule mechanics. Molecular dynamics simulations offered atomic-level descriptions of the forced unfolding. However, experiment and simulation could not be directly compared because they differed in pulling velocity by orders of magnitude. We have developed high-speed force spectroscopy to unfold titin at velocities reached by simulation (~4 millimeters per second). We found that a small β-strand pair of an immunoglobulin domain dynamically unfolds and refolds, buffering pulling forces up to ~100 piconewtons. The distance to the unfolding transition barrier is larger than previously estimated but is in better agreement with atomistic predictions. The ability to directly compare experiment and simulation is likely to be important in studies of biomechanical processes.

publication date

  • January 2013

Research

keywords

  • Academic Article

Identity

Language

  • eng

Digital Object Identifier (DOI)

  • 10.1126/science.1239764

PubMed ID

  • 24202172

Additional Document Info

start page

  • 741

end page

  • 3

volume

  • 342

number

  • 6159