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Buehler MJ, Yung YC. How protein materials balance strength, robustness, and adaptability. HFSP J. 2010;4(1):26-40doi: 10.2976/1.3267779.
Buehler, M. J., & Yung, Y. C. (2010). How protein materials balance strength, robustness, and adaptability. HFSP journal, 4(1), 26-40. https://doi.org/10.2976/1.3267779
Buehler, Markus J, and Yung, Yu Ching. "How protein materials balance strength, robustness, and adaptability." HFSP journal vol. 4,1 (2010): 26-40. doi: https://doi.org/10.2976/1.3267779
Buehler MJ, Yung YC. How protein materials balance strength, robustness, and adaptability. HFSP J. 2010 Feb;4(1):26-40. doi: 10.2976/1.3267779. Epub 2010 Jan 14. PMID: 20676305; PMCID: PMC2880027.
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HFSP J. 2010 Feb;4(1):26-40. doi: 10.2976/1.3267779. Epub 2010 Jan 14.

How protein materials balance strength, robustness, and adaptability.

HFSP journal

Markus J Buehler, Yu Ching Yung

PMID: 20676305 PMCID: PMC2880027 DOI: 10.2976/1.3267779

Abstract

Proteins form the basis of a wide range of biological materials such as hair, skin, bone, spider silk, or cells, which play an important role in providing key functions to biological systems. The focus of this article is to discuss how protein materials are capable of balancing multiple, seemingly incompatible properties such as strength, robustness, and adaptability. To illustrate this, we review bottom-up materiomics studies focused on the mechanical behavior of protein materials at multiple scales, from nano to macro. We focus on alpha-helix based intermediate filament proteins as a model system to explain why the utilization of hierarchical structural features is vital to their ability to combine strength, robustness, and adaptability. Experimental studies demonstrating the activation of angiogenesis, the growth of new blood vessels, are presented as an example of how adaptability of structure in biological tissue is achieved through changes in gene expression that result in an altered material structure. We analyze the concepts in light of the universality and diversity of the structural makeup of protein materials and discuss the findings in the context of potential fundamental evolutionary principles that control their nanoscale structure. We conclude with a discussion of multiscale science in biology and de novo materials design.

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