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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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.
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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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.</description><identifier>ISSN: 0044-8249</identifier><identifier>EISSN: 1521-3757</identifier><identifier>DOI: 10.1002/ange.201602268</identifier><language>eng</language><publisher>Weinheim: Blackwell Publishing Ltd</publisher><subject>Biopolymere ; Chemistry ; Crystal structure ; Density functional theory ; Diffraction ; Elasticity ; Elastizität ; Flexibility ; Helices ; Modulus of elasticity ; Polymers ; Polyprolin ; Proteine ; Spectroscopy ; Spectrum analysis ; Terahertz-Spektroskopie</subject><ispartof>Angewandte Chemie, 2016-06, Vol.128 (24), p.6991-6995</ispartof><rights>2016 The Authors. Published by Wiley-VCH Verlag GmbH & Co. KGaA.</rights><rights>2016 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c2738-cd04f511d41eb9dbe88bb729bf793427f7da411f3659318646dbb91848583a023</citedby><cites>FETCH-LOGICAL-c2738-cd04f511d41eb9dbe88bb729bf793427f7da411f3659318646dbb91848583a023</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1002%2Fange.201602268$$EPDF$$P50$$Gwiley$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1002%2Fange.201602268$$EHTML$$P50$$Gwiley$$Hfree_for_read</linktohtml><link.rule.ids>314,780,784,1417,27924,27925,45574,45575</link.rule.ids></links><search><creatorcontrib>Ruggiero, Michael T.</creatorcontrib><creatorcontrib>Sibik, Juraj</creatorcontrib><creatorcontrib>Orlando, Roberto</creatorcontrib><creatorcontrib>Zeitler, J. Axel</creatorcontrib><creatorcontrib>Korter, Timothy M.</creatorcontrib><title>Measuring the Elasticity of Poly-l-Proline Helices with Terahertz Spectroscopy</title><title>Angewandte Chemie</title><addtitle>Angew. Chem</addtitle><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.
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.</description><subject>Biopolymere</subject><subject>Chemistry</subject><subject>Crystal structure</subject><subject>Density functional theory</subject><subject>Diffraction</subject><subject>Elasticity</subject><subject>Elastizität</subject><subject>Flexibility</subject><subject>Helices</subject><subject>Modulus of elasticity</subject><subject>Polymers</subject><subject>Polyprolin</subject><subject>Proteine</subject><subject>Spectroscopy</subject><subject>Spectrum analysis</subject><subject>Terahertz-Spektroskopie</subject><issn>0044-8249</issn><issn>1521-3757</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2016</creationdate><recordtype>article</recordtype><sourceid>24P</sourceid><sourceid>WIN</sourceid><recordid>eNqFkcFP2zAUhy00JLrClXMkLruk87Od2D4i1KWTuoLUIo6Wk7xQg0k6O1XJ_vq1dEITF07v8n0_vfd7hFwCnQCl7LttH3HCKOSUsVydkBFkDFIuM_mFjCgVIlVM6DPyNcYnSmnOpB6RxS-0cRtc-5j0a0ym3sbeVa4fkq5J7jo_pD69C513LSYz9K7CmOxcv05WGOwaQ_8nWW6w6kMXq24znJPTxvqIF__mmNz_mK5uZun8tvh5cz1PKya5SquaiiYDqAVgqesSlSpLyXTZSM0Fk42srQBoeJ5pDioXeV2WGpRQmeKWMj4m3465m9D93mLszYuLFXpvW-y20YBimZA80wf06gP61G1Du9_OgNRMAoO3wMmRqvaXxICN2QT3YsNggJpDveZQr3mvdy_oo7BzHodPaHO9KKb_u-nRdbHH13fXhmeTy_3DzMOiMMUMVsVips2S_wXBPIyP</recordid><startdate>20160606</startdate><enddate>20160606</enddate><creator>Ruggiero, Michael T.</creator><creator>Sibik, Juraj</creator><creator>Orlando, Roberto</creator><creator>Zeitler, J. Axel</creator><creator>Korter, Timothy M.</creator><general>Blackwell Publishing Ltd</general><general>Wiley Subscription Services, Inc</general><scope>BSCLL</scope><scope>24P</scope><scope>WIN</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7SR</scope><scope>7U5</scope><scope>8BQ</scope><scope>8FD</scope><scope>JG9</scope><scope>L7M</scope></search><sort><creationdate>20160606</creationdate><title>Measuring the Elasticity of Poly-l-Proline Helices with Terahertz Spectroscopy</title><author>Ruggiero, Michael T. ; Sibik, Juraj ; Orlando, Roberto ; Zeitler, J. Axel ; Korter, Timothy M.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c2738-cd04f511d41eb9dbe88bb729bf793427f7da411f3659318646dbb91848583a023</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2016</creationdate><topic>Biopolymere</topic><topic>Chemistry</topic><topic>Crystal structure</topic><topic>Density functional theory</topic><topic>Diffraction</topic><topic>Elasticity</topic><topic>Elastizität</topic><topic>Flexibility</topic><topic>Helices</topic><topic>Modulus of elasticity</topic><topic>Polymers</topic><topic>Polyprolin</topic><topic>Proteine</topic><topic>Spectroscopy</topic><topic>Spectrum analysis</topic><topic>Terahertz-Spektroskopie</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Ruggiero, Michael T.</creatorcontrib><creatorcontrib>Sibik, Juraj</creatorcontrib><creatorcontrib>Orlando, Roberto</creatorcontrib><creatorcontrib>Zeitler, J. Axel</creatorcontrib><creatorcontrib>Korter, Timothy M.</creatorcontrib><collection>Istex</collection><collection>Wiley Online Library (Open Access Collection)</collection><collection>Wiley Online Library Free Content</collection><collection>CrossRef</collection><collection>Engineered Materials Abstracts</collection><collection>Solid State and Superconductivity Abstracts</collection><collection>METADEX</collection><collection>Technology Research Database</collection><collection>Materials Research Database</collection><collection>Advanced Technologies Database with Aerospace</collection><jtitle>Angewandte Chemie</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Ruggiero, Michael T.</au><au>Sibik, Juraj</au><au>Orlando, Roberto</au><au>Zeitler, J. Axel</au><au>Korter, Timothy M.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Measuring the Elasticity of Poly-l-Proline Helices with Terahertz Spectroscopy</atitle><jtitle>Angewandte Chemie</jtitle><addtitle>Angew. Chem</addtitle><date>2016-06-06</date><risdate>2016</risdate><volume>128</volume><issue>24</issue><spage>6991</spage><epage>6995</epage><pages>6991-6995</pages><issn>0044-8249</issn><eissn>1521-3757</eissn><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.
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.</abstract><cop>Weinheim</cop><pub>Blackwell Publishing Ltd</pub><doi>10.1002/ange.201602268</doi><tpages>5</tpages><oa>free_for_read</oa></addata></record> |
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subjects | Biopolymere Chemistry Crystal structure Density functional theory Diffraction Elasticity Elastizität Flexibility Helices Modulus of elasticity Polymers Polyprolin Proteine Spectroscopy Spectrum analysis Terahertz-Spektroskopie |
title | Measuring the Elasticity of Poly-l-Proline Helices with Terahertz Spectroscopy |
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