Measuring the Elasticity of Poly‐l‐Proline Helices with Terahertz Spectroscopy |
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| Authors: | Michael T Ruggiero Dr Juraj Sibik Dr J Axel Zeitler Prof Timothy M Korter |
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| Institution: | 1. Department of Chemistry, Syracuse University, Syracuse, NY, USA;2. Department of Chemical Engineering and Biotechnology, University of Cambridge, New Museums Site, Cambridge, UK;3. F. Hoffmann-La Roche AG, Konzern-Hauptsitz, Basel, Switzerland |
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| Abstract: | The rigidity of poly‐l ‐proline is an important contributor to the stability of many protein secondary structures, where it has been shown to strongly influence bulk flexibility. The experimental Young's moduli of two known poly‐l ‐proline helical forms, right‐handed all‐cis (Form I) and left‐handed all‐trans (Form II), were determined in the crystalline state by using an approach that combines terahertz time‐domain spectroscopy, X‐ray diffraction, and solid‐state density functional theory. Contrary to expectations, the helices were found to be considerably less rigid than many other natural and synthetic polymers, as well as differing greatly from each other, with Young's moduli of 4.9 and 9.6 GPa for Forms I and II, respectively. |
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| Keywords: | biopolymers elasticity polyproline proteins terahertz spectroscopy |
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