Observation of a Silk-Like Crystal Structure in a Genetically Engineered Periodic Polypeptide
A genetically engineered periodic polypeptide consisting of 36 repeats of the octapeptide sequence -(AlaGly) 3 GluGly- has been crystallized from solution in aqueous lithium bromide. Analysis by solid-state nuclear magnetic resonance spectroscopy, vibrational spectroscopy, and wide-angle x-ray diffr...
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| Veröffentlicht in: | Journal of macromolecular science. Part A, Pure and applied chemistry Pure and applied chemistry, 1996-10, Vol.33 (10), p.1389-1398 |
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| Format: | Artikel |
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| container_end_page | 1398 |
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| container_issue | 10 |
| container_start_page | 1389 |
| container_title | Journal of macromolecular science. Part A, Pure and applied chemistry |
| container_volume | 33 |
| creator | Krejchi, Mark T. Atkins, Edward D. T. Fournier, Maurille J. Mason, Thomas L. Tirrell, David A. |
| description | A genetically engineered periodic polypeptide consisting of 36 repeats of the octapeptide sequence -(AlaGly)
3
GluGly- has been crystallized from solution in aqueous lithium bromide. Analysis by solid-state nuclear magnetic resonance spectroscopy, vibrational spectroscopy, and wide-angle x-ray diffraction reveals a crystal structure analogous to that obtained when silk solutions are allowed to dry under quiescent conditions, i.e., the silk I structure. Previous analyses of the same polymer have demonstrated an antiparallel β-sheet architecture (silk II structure) in samples crystallized from formic acid. These results illustrate the potential for controlling the solid-state structures and properties of genetically engineered materials through selection of appropriate processing and crystallization conditions. |
| doi_str_mv | 10.1080/10601329608014915 |
| format | Article |
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3
GluGly- has been crystallized from solution in aqueous lithium bromide. Analysis by solid-state nuclear magnetic resonance spectroscopy, vibrational spectroscopy, and wide-angle x-ray diffraction reveals a crystal structure analogous to that obtained when silk solutions are allowed to dry under quiescent conditions, i.e., the silk I structure. Previous analyses of the same polymer have demonstrated an antiparallel β-sheet architecture (silk II structure) in samples crystallized from formic acid. These results illustrate the potential for controlling the solid-state structures and properties of genetically engineered materials through selection of appropriate processing and crystallization conditions.</description><identifier>ISSN: 1060-1325</identifier><identifier>EISSN: 1520-5738</identifier><identifier>DOI: 10.1080/10601329608014915</identifier><identifier>CODEN: JSPCE6</identifier><language>eng</language><publisher>Colchester: Taylor & Francis Group</publisher><subject>Aminoacid polymers ; Applied sciences ; Exact sciences and technology ; Physicochemistry of polymers ; Synthetic biopolymers</subject><ispartof>Journal of macromolecular science. Part A, Pure and applied chemistry, 1996-10, Vol.33 (10), p.1389-1398</ispartof><rights>Copyright Taylor & Francis Group, LLC 1996</rights><rights>1996 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c422t-377dd41fb4edcbff1cecc0332eec0b1ef1715f18f303779eb4a1ac7cdaf9b37a3</citedby><cites>FETCH-LOGICAL-c422t-377dd41fb4edcbff1cecc0332eec0b1ef1715f18f303779eb4a1ac7cdaf9b37a3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.tandfonline.com/doi/pdf/10.1080/10601329608014915$$EPDF$$P50$$Ginformaworld$$H</linktopdf><linktohtml>$$Uhttps://www.tandfonline.com/doi/full/10.1080/10601329608014915$$EHTML$$P50$$Ginformaworld$$H</linktohtml><link.rule.ids>309,310,314,776,780,785,786,23909,23910,25118,27901,27902,59620,60409</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=3221036$$DView record in Pascal Francis$$Hfree_for_read</backlink></links><search><creatorcontrib>Krejchi, Mark T.</creatorcontrib><creatorcontrib>Atkins, Edward D. T.</creatorcontrib><creatorcontrib>Fournier, Maurille J.</creatorcontrib><creatorcontrib>Mason, Thomas L.</creatorcontrib><creatorcontrib>Tirrell, David A.</creatorcontrib><title>Observation of a Silk-Like Crystal Structure in a Genetically Engineered Periodic Polypeptide</title><title>Journal of macromolecular science. Part A, Pure and applied chemistry</title><description>A genetically engineered periodic polypeptide consisting of 36 repeats of the octapeptide sequence -(AlaGly)
3
GluGly- has been crystallized from solution in aqueous lithium bromide. Analysis by solid-state nuclear magnetic resonance spectroscopy, vibrational spectroscopy, and wide-angle x-ray diffraction reveals a crystal structure analogous to that obtained when silk solutions are allowed to dry under quiescent conditions, i.e., the silk I structure. Previous analyses of the same polymer have demonstrated an antiparallel β-sheet architecture (silk II structure) in samples crystallized from formic acid. These results illustrate the potential for controlling the solid-state structures and properties of genetically engineered materials through selection of appropriate processing and crystallization conditions.</description><subject>Aminoacid polymers</subject><subject>Applied sciences</subject><subject>Exact sciences and technology</subject><subject>Physicochemistry of polymers</subject><subject>Synthetic biopolymers</subject><issn>1060-1325</issn><issn>1520-5738</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1996</creationdate><recordtype>article</recordtype><recordid>eNp1kEFLw0AQhYMoWKs_wNsexFt0J5s0CXiRUqtQaKF6lLDZzMrabTbubpT8e7e0ehFPM8N87w3zougS6A3Qgt4CnVBgSTkJA6QlZEfRCLKExlnOiuPQh30cgOw0OnPundIdDaPodVk7tJ_cK9MSIwkna6U38UJtkEzt4DzXZO1tL3xvkag2AHNs0SvBtR7IrH1TLaLFhqzQKtMoQVZGDx12XjV4Hp1Irh1eHOo4enmYPU8f48Vy_jS9X8QiTRIfszxvmhRknWIjailBoBCUsQRR0BpQQg6ZhEIyGtAS65QDF7louCxrlnM2jq73vp01Hz06X22VE6g1b9H0roKsoHmaZAGEPSiscc6irDqrttwOFdBqF2T1J8iguTqYcxe-lpa3QrlfIUsSoGwSsLs9plpp7JZ_GaubyvNBG_ujYf9f-QZJ-4a3</recordid><startdate>19961001</startdate><enddate>19961001</enddate><creator>Krejchi, Mark T.</creator><creator>Atkins, Edward D. T.</creator><creator>Fournier, Maurille J.</creator><creator>Mason, Thomas L.</creator><creator>Tirrell, David A.</creator><general>Taylor & Francis Group</general><general>Taylor & Francis</general><scope>IQODW</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7QO</scope><scope>8FD</scope><scope>FR3</scope><scope>P64</scope></search><sort><creationdate>19961001</creationdate><title>Observation of a Silk-Like Crystal Structure in a Genetically Engineered Periodic Polypeptide</title><author>Krejchi, Mark T. ; Atkins, Edward D. T. ; Fournier, Maurille J. ; Mason, Thomas L. ; Tirrell, David A.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c422t-377dd41fb4edcbff1cecc0332eec0b1ef1715f18f303779eb4a1ac7cdaf9b37a3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1996</creationdate><topic>Aminoacid polymers</topic><topic>Applied sciences</topic><topic>Exact sciences and technology</topic><topic>Physicochemistry of polymers</topic><topic>Synthetic biopolymers</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Krejchi, Mark T.</creatorcontrib><creatorcontrib>Atkins, Edward D. T.</creatorcontrib><creatorcontrib>Fournier, Maurille J.</creatorcontrib><creatorcontrib>Mason, Thomas L.</creatorcontrib><creatorcontrib>Tirrell, David A.</creatorcontrib><collection>Pascal-Francis</collection><collection>CrossRef</collection><collection>Biotechnology Research Abstracts</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><jtitle>Journal of macromolecular science. Part A, Pure and applied chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Krejchi, Mark T.</au><au>Atkins, Edward D. T.</au><au>Fournier, Maurille J.</au><au>Mason, Thomas L.</au><au>Tirrell, David A.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Observation of a Silk-Like Crystal Structure in a Genetically Engineered Periodic Polypeptide</atitle><jtitle>Journal of macromolecular science. Part A, Pure and applied chemistry</jtitle><date>1996-10-01</date><risdate>1996</risdate><volume>33</volume><issue>10</issue><spage>1389</spage><epage>1398</epage><pages>1389-1398</pages><issn>1060-1325</issn><eissn>1520-5738</eissn><coden>JSPCE6</coden><abstract>A genetically engineered periodic polypeptide consisting of 36 repeats of the octapeptide sequence -(AlaGly)
3
GluGly- has been crystallized from solution in aqueous lithium bromide. Analysis by solid-state nuclear magnetic resonance spectroscopy, vibrational spectroscopy, and wide-angle x-ray diffraction reveals a crystal structure analogous to that obtained when silk solutions are allowed to dry under quiescent conditions, i.e., the silk I structure. Previous analyses of the same polymer have demonstrated an antiparallel β-sheet architecture (silk II structure) in samples crystallized from formic acid. These results illustrate the potential for controlling the solid-state structures and properties of genetically engineered materials through selection of appropriate processing and crystallization conditions.</abstract><cop>Colchester</cop><pub>Taylor & Francis Group</pub><doi>10.1080/10601329608014915</doi><tpages>10</tpages></addata></record> |
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| ispartof | Journal of macromolecular science. Part A, Pure and applied chemistry, 1996-10, Vol.33 (10), p.1389-1398 |
| issn | 1060-1325 1520-5738 |
| language | eng |
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| source | Taylor & Francis |
| subjects | Aminoacid polymers Applied sciences Exact sciences and technology Physicochemistry of polymers Synthetic biopolymers |
| title | Observation of a Silk-Like Crystal Structure in a Genetically Engineered Periodic Polypeptide |
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