Measuring the Elasticity of Poly-l-Proline Helices with Terahertz Spectroscopy
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‐han...
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Veröffentlicht in: | Angewandte Chemie 2016-06, Vol.128 (24), p.6991-6995 |
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Sprache: | eng |
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Zusammenfassung: | 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.
Die experimentellen Young‐Moduln der zwei bekannten helikalen Formen von Poly‐l‐prolin wurden durch eine Kombination aus zeitabhängiger Terahertz‐Spektroskopie, Röntgenbeugung und Festkörper‐DFT‐Theorie bestimmt. Entgegen der Erwartung zeigt sich, dass die Helizes weniger starr sind als viele andere natürliche und synthetische Polymere und sich stark voneinander unterscheiden. |
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ISSN: | 0044-8249 1521-3757 |
DOI: | 10.1002/ange.201602268 |