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Protein's strength lies in h-bond cooperation
Date:2/14/2008

four hydrogen bonds are the most common conformation among all beta-structured proteins, including those comprising muscle tissue, according to experimental proteomics data on protein structures in the Protein Data Bank.

This correlation of a common geometric configuration among beta sheetswhich are one of the two most prevalent protein structures in existencesuggests that a proteins strength is an important evolutionary driving force behind its physical design. The researchers observed the same behavior in similar small clusters in alpha-helical structural proteins, the other most prevalent protein, but havent yet studied those assemblies in detail.

On the other hand, synthetic materials like steel have a very different and crystalline structure held together by the stronger glue of metallic bonds. Because steel and other synthetic materials tend to be dense, and therefore heavy, they consume a good deal of energy in manufacturing and transport.

Metals are configured with bonds that are much stronger and require a much greater force to break, said Buehler. However, the crystalline lattice of a metals structure is never perfect; it contains defects that effectively reduce the materials strength quite drastically. When you place a load on the metal, the defect can fail, possibly causing a crack to propagate. In proteins beta sheets, the confined nature of the hydrogen bond clusters helps to dissipate the energy without compromising the strength of the material. This shows the amazing ingenuity and efficiency of natural materials.


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Contact: Denise Brehm
brehm@mit.edu
617-253-8069
Massachusetts Institute of Technology, Department of Civil and Environmental Engineering
Source:Eurekalert

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