Spring mechanics of α-helical polypeptide
Open Access
- 1 November 2000
- journal article
- Published by Oxford University Press (OUP) in Protein Engineering, Design and Selection
- Vol. 13 (11) , 763-770
- https://doi.org/10.1093/protein/13.11.763
Abstract
To design protein- and polymer-based micro-machineries, it is important to understand the mechanical properties of basic structural elements such as the α-helix of polypeptides. We employed the force measurement mode of an atomic force microscope (AFM) to investigate the spring mechanics of poly-l-glutamic acid (PGA) in its helical and randomly coiled states. After covalently anchoring the polypeptide between a silicon substrate and an AFM tip, the force required to stretch the polymer was measured. The results indicated that PGA in its helical conformation could be stretched almost fully with a continuous increase in the stretching force, suggesting that it can be used as a reliable coil-spring in the future design of spring-loaded molecular machineries.Keywords
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