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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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Autores principales: Ruggiero, Michael T., Sibik, Juraj, Orlando, Roberto, Zeitler, J. Axel, Korter, Timothy M.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: John Wiley and Sons Inc. 2016
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4999051/
https://www.ncbi.nlm.nih.gov/pubmed/27121300
http://dx.doi.org/10.1002/anie.201602268
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author Ruggiero, Michael T.
Sibik, Juraj
Orlando, Roberto
Zeitler, J. Axel
Korter, Timothy M.
author_facet Ruggiero, Michael T.
Sibik, Juraj
Orlando, Roberto
Zeitler, J. Axel
Korter, Timothy M.
author_sort Ruggiero, Michael T.
collection PubMed
description 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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spelling pubmed-49990512016-09-13 Measuring the Elasticity of Poly‐l‐Proline Helices with Terahertz Spectroscopy Ruggiero, Michael T. Sibik, Juraj Orlando, Roberto Zeitler, J. Axel Korter, Timothy M. Angew Chem Int Ed Engl Communications 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. John Wiley and Sons Inc. 2016-04-28 2016-06-06 /pmc/articles/PMC4999051/ /pubmed/27121300 http://dx.doi.org/10.1002/anie.201602268 Text en © 2016 The Authors. Published by Wiley-VCH Verlag GmbH & Co. KGaA. This is an open access article under the terms of the Creative Commons Attribution (http://creativecommons.org/licenses/by/4.0/) License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited.
spellingShingle Communications
Ruggiero, Michael T.
Sibik, Juraj
Orlando, Roberto
Zeitler, J. Axel
Korter, Timothy M.
Measuring the Elasticity of Poly‐l‐Proline Helices with Terahertz Spectroscopy
title Measuring the Elasticity of Poly‐l‐Proline Helices with Terahertz Spectroscopy
title_full Measuring the Elasticity of Poly‐l‐Proline Helices with Terahertz Spectroscopy
title_fullStr Measuring the Elasticity of Poly‐l‐Proline Helices with Terahertz Spectroscopy
title_full_unstemmed Measuring the Elasticity of Poly‐l‐Proline Helices with Terahertz Spectroscopy
title_short Measuring the Elasticity of Poly‐l‐Proline Helices with Terahertz Spectroscopy
title_sort measuring the elasticity of poly‐l‐proline helices with terahertz spectroscopy
topic Communications
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4999051/
https://www.ncbi.nlm.nih.gov/pubmed/27121300
http://dx.doi.org/10.1002/anie.201602268
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