Asymptotic strength limit of hydrogen bond assemblies in proteins at vanishing pulling rates

Sinan Keten*, Markus J. Buehler

*Corresponding author for this work

Research output: Chapter in Book/Report/Conference proceedingConference contribution

Abstract

Experimental and computational studies on mechanical unfolding of proteins suggest that rupture forces approach a limiting value of a few hundred pN at vanishing pulling velocities. We develop a fracture mechanics based theoretical framework that considers the free energy competition between entropic elasticity of polypeptide chains and rupture of peptide hydrogen bonds, which we use here to provide an explanation for the intrinsic strength limit of proteins. Our analysis predicts that individual protein domains stabilized by hydrogen bonds can not exhibit rupture forces larger than ≈ 200 pN, regardless of the presence of a large number of hydrogen bonds. This result explains a wide range of experimental and computational observations.

Original languageEnglish (US)
Title of host publicationMaterials Research Society Symposium Proceedings - Protein and Peptide Engineering for Therapeutic and Functional Materials
Pages23-28
Number of pages6
StatePublished - Dec 1 2008
EventProtein and Peptide Engineering for Therapeutic and Functional Materials - Boston, MA, United States
Duration: Nov 26 2007Nov 30 2007

Publication series

NameMaterials Research Society Symposium Proceedings
Volume1062
ISSN (Print)0272-9172

Other

OtherProtein and Peptide Engineering for Therapeutic and Functional Materials
CountryUnited States
CityBoston, MA
Period11/26/0711/30/07

ASJC Scopus subject areas

  • Materials Science(all)
  • Condensed Matter Physics
  • Mechanics of Materials
  • Mechanical Engineering

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