Direct determination of helix structures involved in the screw‐sense reversal of poly(β‐phenylpropyl l‐aspartate) by synchrotron X‐ray diffraction
The helix‐sense reversal of poly(β‐phenylpropyl l‐aspartate) (3PLA) in the solid state was studied by synchrotron wide‐angle X‐ray diffraction and small‐angle X‐ray scattering. The direct determination of the characteristic helical pitch before and after the transition revealed that the transition t...
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creator | Orito, Yuki Masunaga, Hiroyasu Furuya, Hidemine Abe, Akihiro |
description | The helix‐sense reversal of poly(β‐phenylpropyl l‐aspartate) (3PLA) in the solid state was studied by synchrotron wide‐angle X‐ray diffraction and small‐angle X‐ray scattering. The direct determination of the characteristic helical pitch before and after the transition revealed that the transition takes place reversibly between the two α‐helices having opposite screw‐sense during the heating and cooling cycle. While the hexagonal packing remains unaltered, the helix‐sense inversion causes discontinuous changes in the molecular arrangement and, by extension, the crystalline dimension. In this study, another transition was detected at a higher temperature from the left‐handed α‐helix to the π‐helix, the molecular chirality being unaffected.
Helix transition of poly(β‐phenylpropyl l‐aspartate) in the solid state was studied by synchrotron WAXD/SAXS. The unit heights characterizing the helix structures were directly observed. A left‐handed α‐helix was formed after helix‐sense inversion. |
doi_str_mv | 10.1002/psc.3311 |
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Helix transition of poly(β‐phenylpropyl l‐aspartate) in the solid state was studied by synchrotron WAXD/SAXS. The unit heights characterizing the helix structures were directly observed. A left‐handed α‐helix was formed after helix‐sense inversion.</description><identifier>ISSN: 1075-2617</identifier><identifier>EISSN: 1099-1387</identifier><identifier>DOI: 10.1002/psc.3311</identifier><identifier>PMID: 33605058</identifier><language>eng</language><publisher>England: Wiley Subscription Services, Inc</publisher><subject>Chirality ; Helices ; helix structure ; helix–helix transition ; High temperature ; Peptides ; poly(β‐phenylpropyl l‐aspartate) ; synchrotron X‐ray diffraction ; Synchrotrons ; X-ray diffraction</subject><ispartof>Journal of peptide science, 2021-06, Vol.27 (6), p.e3311-n/a</ispartof><rights>2021 European Peptide Society and John Wiley & Sons, Ltd.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c3931-da337f293eb7282d7ce7371fa15a776aeb94b0ab62bc154e1bf894b575947d033</citedby><cites>FETCH-LOGICAL-c3931-da337f293eb7282d7ce7371fa15a776aeb94b0ab62bc154e1bf894b575947d033</cites><orcidid>0000-0003-4527-2264</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1002%2Fpsc.3311$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1002%2Fpsc.3311$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,776,780,1411,27901,27902,45550,45551</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/33605058$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Orito, Yuki</creatorcontrib><creatorcontrib>Masunaga, Hiroyasu</creatorcontrib><creatorcontrib>Furuya, Hidemine</creatorcontrib><creatorcontrib>Abe, Akihiro</creatorcontrib><title>Direct determination of helix structures involved in the screw‐sense reversal of poly(β‐phenylpropyl l‐aspartate) by synchrotron X‐ray diffraction</title><title>Journal of peptide science</title><addtitle>J Pept Sci</addtitle><description>The helix‐sense reversal of poly(β‐phenylpropyl l‐aspartate) (3PLA) in the solid state was studied by synchrotron wide‐angle X‐ray diffraction and small‐angle X‐ray scattering. The direct determination of the characteristic helical pitch before and after the transition revealed that the transition takes place reversibly between the two α‐helices having opposite screw‐sense during the heating and cooling cycle. While the hexagonal packing remains unaltered, the helix‐sense inversion causes discontinuous changes in the molecular arrangement and, by extension, the crystalline dimension. In this study, another transition was detected at a higher temperature from the left‐handed α‐helix to the π‐helix, the molecular chirality being unaffected.
Helix transition of poly(β‐phenylpropyl l‐aspartate) in the solid state was studied by synchrotron WAXD/SAXS. The unit heights characterizing the helix structures were directly observed. A left‐handed α‐helix was formed after helix‐sense inversion.</description><subject>Chirality</subject><subject>Helices</subject><subject>helix structure</subject><subject>helix–helix transition</subject><subject>High temperature</subject><subject>Peptides</subject><subject>poly(β‐phenylpropyl l‐aspartate)</subject><subject>synchrotron X‐ray diffraction</subject><subject>Synchrotrons</subject><subject>X-ray diffraction</subject><issn>1075-2617</issn><issn>1099-1387</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2021</creationdate><recordtype>article</recordtype><recordid>eNp1kc-K1TAUxoM4OOMo-AQScDMuOiZN07RLuf4ZYUBBBXchTU-5GXKbepLesTsfwb1v4YP4EPMkpjOjguAqh_P98p0PPkIecXbKGSufTdGeCsH5HXLEWdsWXDTq7jorWZQ1V4fkfowXjGVN1vfIoRA1k0w2R-T7C4dgE-0hAe7caJILIw0D3YJ3X2hMONs0I0Tqxn3we-jzQNMWaLQIl1dfv0UYI1CEPWA0fv06Bb-c_PyRtWkL4-InDNPiqc8LEyeDySR4SruFxmW0WwwJ88lPWUWz0N4NAxq7xnhADgbjIzy8fY_Jx1cvP2zOivO3r99snp8XVrSCF70RQg1lK6BTZVP2yoISig-GS6NUbaBrq46Zri47y2UFvBuavJFKtpXqmRDH5OTGNwf9PENMeueiBe_NCGGOuqxa3kpRcZXRJ_-gF2HGMafTpeSNFEzU1V9DiyFGhEFP6HYGF82ZXgvTuTC9FpbRx7eGc7eD_g_4u6EMFDfApfOw_NdIv3u_uTb8BdXupsE</recordid><startdate>202106</startdate><enddate>202106</enddate><creator>Orito, Yuki</creator><creator>Masunaga, Hiroyasu</creator><creator>Furuya, Hidemine</creator><creator>Abe, Akihiro</creator><general>Wiley Subscription Services, Inc</general><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7QO</scope><scope>7TK</scope><scope>8FD</scope><scope>FR3</scope><scope>K9.</scope><scope>P64</scope><scope>7X8</scope><orcidid>https://orcid.org/0000-0003-4527-2264</orcidid></search><sort><creationdate>202106</creationdate><title>Direct determination of helix structures involved in the screw‐sense reversal of poly(β‐phenylpropyl l‐aspartate) by synchrotron X‐ray diffraction</title><author>Orito, Yuki ; Masunaga, Hiroyasu ; Furuya, Hidemine ; Abe, Akihiro</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c3931-da337f293eb7282d7ce7371fa15a776aeb94b0ab62bc154e1bf894b575947d033</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2021</creationdate><topic>Chirality</topic><topic>Helices</topic><topic>helix structure</topic><topic>helix–helix transition</topic><topic>High temperature</topic><topic>Peptides</topic><topic>poly(β‐phenylpropyl l‐aspartate)</topic><topic>synchrotron X‐ray diffraction</topic><topic>Synchrotrons</topic><topic>X-ray diffraction</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Orito, Yuki</creatorcontrib><creatorcontrib>Masunaga, Hiroyasu</creatorcontrib><creatorcontrib>Furuya, Hidemine</creatorcontrib><creatorcontrib>Abe, Akihiro</creatorcontrib><collection>PubMed</collection><collection>CrossRef</collection><collection>Biotechnology Research Abstracts</collection><collection>Neurosciences Abstracts</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Journal of peptide science</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Orito, Yuki</au><au>Masunaga, Hiroyasu</au><au>Furuya, Hidemine</au><au>Abe, Akihiro</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Direct determination of helix structures involved in the screw‐sense reversal of poly(β‐phenylpropyl l‐aspartate) by synchrotron X‐ray diffraction</atitle><jtitle>Journal of peptide science</jtitle><addtitle>J Pept Sci</addtitle><date>2021-06</date><risdate>2021</risdate><volume>27</volume><issue>6</issue><spage>e3311</spage><epage>n/a</epage><pages>e3311-n/a</pages><issn>1075-2617</issn><eissn>1099-1387</eissn><abstract>The helix‐sense reversal of poly(β‐phenylpropyl l‐aspartate) (3PLA) in the solid state was studied by synchrotron wide‐angle X‐ray diffraction and small‐angle X‐ray scattering. The direct determination of the characteristic helical pitch before and after the transition revealed that the transition takes place reversibly between the two α‐helices having opposite screw‐sense during the heating and cooling cycle. While the hexagonal packing remains unaltered, the helix‐sense inversion causes discontinuous changes in the molecular arrangement and, by extension, the crystalline dimension. In this study, another transition was detected at a higher temperature from the left‐handed α‐helix to the π‐helix, the molecular chirality being unaffected.
Helix transition of poly(β‐phenylpropyl l‐aspartate) in the solid state was studied by synchrotron WAXD/SAXS. The unit heights characterizing the helix structures were directly observed. A left‐handed α‐helix was formed after helix‐sense inversion.</abstract><cop>England</cop><pub>Wiley Subscription Services, Inc</pub><pmid>33605058</pmid><doi>10.1002/psc.3311</doi><tpages>6</tpages><orcidid>https://orcid.org/0000-0003-4527-2264</orcidid></addata></record> |
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subjects | Chirality Helices helix structure helix–helix transition High temperature Peptides poly(β‐phenylpropyl l‐aspartate) synchrotron X‐ray diffraction Synchrotrons X-ray diffraction |
title | Direct determination of helix structures involved in the screw‐sense reversal of poly(β‐phenylpropyl l‐aspartate) by synchrotron X‐ray diffraction |
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