Nanomechanics of Single Biomacromolecules



Single-molecule force spectroscopy has provided tremendous insights into the mechanical characteristics of biomacromolecules including proteins, nucleic acids, and sugars. This review provides the instrumentation framework for single-molecule force spectroscopy using atomic force microscopy and the experimental procedures for determining nanomechanics of biomacromolecules. The characteristic parameters determined by single-molecule force spectroscopy of proteins (unfolding forces, intrinsic unfolding/refolding rates, transition state distances, binding affinities), nucleic acids (elastic modulus, persistence length, overstretching percentages, plateau force levels), and sugars (force spectra) from the past 20 years are tabulated and their applications are discussed.


Atomic force microscopy Force spectroscopy Nanomaterials Nanomechanics Protein folding Single molecules 


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Copyright information

© Springer-Verlag Berlin Heidelberg 2014

Authors and Affiliations

  • Qing Li
    • 1
  • Zackary N. Scholl
    • 2
  • Piotr E. Marszalek
    • 1
  1. 1.Department of Mechanical Engineering and Materials ScienceCenter for Biologically Inspired Materials and Material Systems, and Duke UniversityDurhamUSA
  2. 2.Program in Computational Biology and BioinformaticsDuke UniversityDurhamUSA

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