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Protein Engineering, Vol. 13, No. 11, 763-770, November 2000
© 2000 Oxford University Press

Spring mechanics of {alpha}-helical polypeptide

Alimjan Idiris, Mohammad Taufiq Alam and Atsushi Ikai,1

Laboratory of Biodynamics, Faculty of Bioscience and Biotechnology, Tokyo Institute of Technology, 4259 Nagatsuta, Midori-ku, Yokohama226-8501, Japan

To design protein- and polymer-based micro-machineries, it is important to understand the mechanical properties of basic structural elements such as the {alpha}-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.


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