Measuring the Elasticity of Poly-l-Proline Helices with Terahertz Spectroscopy
Published version
Peer-reviewed
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Type
Article
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Authors
Ruggiero, Michael T
Sibik, Juraj
Orlando, Roberto
Zeitler, J Axel
Korter, Timothy M
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
spectroscopy, elasticity, proteins, biopolymer, density functional theory
Journal Title
Angewandte Chemie
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Journal ISSN
0044-8249
1521-3757
1521-3757
Volume Title
128
Publisher
Wiley
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Sponsorship
Engineering and Physical Sciences Research Council (EP/J007803/1)
M.T.R. and T.M.K acknowledge the support of a grant from the National Science Foundation (CHE-1301068). T.M.K. would like to acknowledge the Royal Society International Exchanges Scheme as well as the Royal Society of Chemistry JWT Jones Travelling Fellowship for support. J.S. and J.A.Z. would like to acknowledge the U.K. Engineering and Physical Sciences Research Council (EP/J007803/1) for funding.