ArticleProceedings of the National Academy of Sciences of the United States of America2007
Hierarchies, multiple energy barriers, and robustness govern the fracture mechanics of alpha-helical and beta-sheet protein domains.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.
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43 citing papers in PubMed.
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- A High Coordination of Cross-Links Is Beneficial for the Strength of Cross-Linked Fibers.Biomimetics (Basel, Switzerland) · 2019Article
- Mechanical Deformation Mechanisms and Properties of Prion Fibrils Probed by Atomistic Simulations.Nanoscale research letters · 2017Article
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- Effect of Terminal Modification on the Molecular Assembly and Mechanical Properties of Protein-Based Block Copolymers.Macromolecular bioscience · 2017Article
- Nanomechanical properties of MscL α helices: A steered molecular dynamics study.Channels (Austin, Tex.) · 2017Article
- Molecular level detection and localization of mechanical damage in collagen enabled by collagen hybridizing peptides.Nature communications · 2017Article
- The Gearbox of the Bacterial Flagellar Motor Switch.Structure (London, England : 1993) · 2016Article
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4 authors.
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Abstract
The fundamental fracture mechanisms of biological protein materials remain largely unknown, in part, because of a lack of understanding of how individual protein building blocks respond to mechanical load. For instance, it remains controversial whether the free energy landscape of the unfolding behavior of proteins consists of multiple, discrete transition states or the location of the transition state changes continuously with the pulling velocity. This lack in understanding has thus far prevented us from developing predictive strength models of protein materials. Here, we report direct atomistic simulation that over four orders of magnitude in time scales of the unfolding behavior of alpha-helical (AH) and beta-sheet (BS) domains, the key building blocks of hair, hoof, and wool as well as spider silk, amyloids, and titin. We find that two discrete transition states corresponding to two fracture mechanisms exist. Whereas the unfolding mechanism at fast pulling rates is sequential rupture of individual hydrogen bonds (HBs), unfolding at slow pulling rates proceeds by simultaneous rupture of several HBs. We derive the hierarchical Bell model, a theory that explicitly considers the hierarchical architecture of proteins, providing a rigorous structure-property relationship. We exemplify our model in a study of AHs, and show that 3-4 parallel HBs per turn are favorable in light of the protein's mechanical and thermodynamical stability, in agreement with experimental findings that AHs feature 3.6 HBs per turn. Our results provide evidence that the molecular structure of AHs maximizes its robustness at minimal use of building materials.
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