Spring mechanics of alpha-helical polypeptide

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...

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Bibliographic Details
Published inProtein engineering Vol. 13; no. 11; pp. 763 - 770
Main Authors Idiris, A, Alam, M T, Ikai, A
Format Journal Article
LanguageEnglish
Published England 01.11.2000
Subjects
Biomechanical Phenomena
Circular Dichroism
Microscopy, Atomic Force
Models, Molecular
Peptides - chemistry
Polyglutamic Acid - chemistry
Protein Structure, Secondary
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Summary: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.
ISSN:0269-2139
1741-0126
1741-0134
DOI:10.1093/protein/13.11.763