Carbonization of a stable β-sheet-rich silk protein into a pseudographitic pyroprotein
DC Field | Value | Language |
---|---|---|
dc.contributor.author | Cho, S.Y. | - |
dc.contributor.author | Yun, Y.S. | - |
dc.contributor.author | Lee, S. | - |
dc.contributor.author | Jang, D. | - |
dc.contributor.author | Park, K.-Y. | - |
dc.contributor.author | Kim, J.K. | - |
dc.contributor.author | Kim, B.H. | - |
dc.contributor.author | Kang, K. | - |
dc.contributor.author | Kaplan, D.L. | - |
dc.contributor.author | Jin, H.-J. | - |
dc.date.accessioned | 2021-09-04T23:58:26Z | - |
dc.date.available | 2021-09-04T23:58:26Z | - |
dc.date.created | 2021-06-17 | - |
dc.date.issued | 2015 | - |
dc.identifier.issn | 2041-1723 | - |
dc.identifier.uri | https://scholar.korea.ac.kr/handle/2021.sw.korea/95933 | - |
dc.description.abstract | Silk proteins are of great interest to the scientific community owing to their unique mechanical properties and interesting biological functionality. In addition, the silk proteins are not burned out following heating, rather they are transformed into a carbonaceous solid, pyroprotein; several studies have identified potential carbon precursors for state-of-the-art technologies. However, no mechanism for the carbonization of proteins has yet been reported. Here we examine the structural and chemical changes of silk proteins systematically at temperatures above the onset of thermal degradation. We find that the β-sheet structure is transformed into an sp 2 -hybridized carbon hexagonal structure by simple heating to 350 °C. The pseudographitic crystalline layers grew to form highly ordered graphitic structures following further heating to 2,800 °C. Our results provide a mechanism for the thermal transition of the protein and demonstrate a potential strategy for designing pyroproteins using a clean system with a catalyst-free aqueous wet process for in vivo applications. © 2015 Macmillan Publishers Limited. All rights reserved. | - |
dc.language | English | - |
dc.language.iso | en | - |
dc.publisher | Nature Publishing Group | - |
dc.subject | carbon | - |
dc.subject | protein | - |
dc.subject | pseudographitic pyroprotein | - |
dc.subject | silk protein | - |
dc.subject | unclassified drug | - |
dc.subject | carbon | - |
dc.subject | fibroin | - |
dc.subject | silk | - |
dc.subject | catalyst | - |
dc.subject | degradation | - |
dc.subject | protein | - |
dc.subject | temperature gradient | - |
dc.subject | Article | - |
dc.subject | beta sheet | - |
dc.subject | carbonization | - |
dc.subject | catalyst | - |
dc.subject | crystallization | - |
dc.subject | heating | - |
dc.subject | hydrogen bond | - |
dc.subject | nonhuman | - |
dc.subject | protein degradation | - |
dc.subject | protein modification | - |
dc.subject | protein stability | - |
dc.subject | protein structure | - |
dc.subject | pyrolysis | - |
dc.subject | scanning electron microscopy | - |
dc.subject | temperature | - |
dc.subject | thermogravimetry | - |
dc.subject | thermostability | - |
dc.subject | X ray photoelectron spectroscopy | - |
dc.subject | animal | - |
dc.subject | Bombyx | - |
dc.subject | catalysis | - |
dc.subject | chemistry | - |
dc.subject | differential scanning calorimetry | - |
dc.subject | heat | - |
dc.subject | infrared spectroscopy | - |
dc.subject | protein secondary structure | - |
dc.subject | X ray diffraction | - |
dc.subject | Animals | - |
dc.subject | Bombyx | - |
dc.subject | Calorimetry, Differential Scanning | - |
dc.subject | Carbon | - |
dc.subject | Catalysis | - |
dc.subject | Crystallization | - |
dc.subject | Fibroins | - |
dc.subject | Hot Temperature | - |
dc.subject | Microscopy, Electron, Scanning | - |
dc.subject | Protein Structure, Secondary | - |
dc.subject | Silk | - |
dc.subject | Spectroscopy, Fourier Transform Infrared | - |
dc.subject | X-Ray Diffraction | - |
dc.title | Carbonization of a stable β-sheet-rich silk protein into a pseudographitic pyroprotein | - |
dc.type | Article | - |
dc.contributor.affiliatedAuthor | Yun, Y.S. | - |
dc.identifier.doi | 10.1038/ncomms8145 | - |
dc.identifier.scopusid | 2-s2.0-84930221997 | - |
dc.identifier.bibliographicCitation | Nature Communications, v.6 | - |
dc.relation.isPartOf | Nature Communications | - |
dc.citation.title | Nature Communications | - |
dc.citation.volume | 6 | - |
dc.type.rims | ART | - |
dc.type.docType | Article | - |
dc.description.journalClass | 1 | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
dc.subject.keywordPlus | carbon | - |
dc.subject.keywordPlus | protein | - |
dc.subject.keywordPlus | pseudographitic pyroprotein | - |
dc.subject.keywordPlus | silk protein | - |
dc.subject.keywordPlus | unclassified drug | - |
dc.subject.keywordPlus | carbon | - |
dc.subject.keywordPlus | fibroin | - |
dc.subject.keywordPlus | silk | - |
dc.subject.keywordPlus | catalyst | - |
dc.subject.keywordPlus | degradation | - |
dc.subject.keywordPlus | protein | - |
dc.subject.keywordPlus | temperature gradient | - |
dc.subject.keywordPlus | Article | - |
dc.subject.keywordPlus | beta sheet | - |
dc.subject.keywordPlus | carbonization | - |
dc.subject.keywordPlus | catalyst | - |
dc.subject.keywordPlus | crystallization | - |
dc.subject.keywordPlus | heating | - |
dc.subject.keywordPlus | hydrogen bond | - |
dc.subject.keywordPlus | nonhuman | - |
dc.subject.keywordPlus | protein degradation | - |
dc.subject.keywordPlus | protein modification | - |
dc.subject.keywordPlus | protein stability | - |
dc.subject.keywordPlus | protein structure | - |
dc.subject.keywordPlus | pyrolysis | - |
dc.subject.keywordPlus | scanning electron microscopy | - |
dc.subject.keywordPlus | temperature | - |
dc.subject.keywordPlus | thermogravimetry | - |
dc.subject.keywordPlus | thermostability | - |
dc.subject.keywordPlus | X ray photoelectron spectroscopy | - |
dc.subject.keywordPlus | animal | - |
dc.subject.keywordPlus | Bombyx | - |
dc.subject.keywordPlus | catalysis | - |
dc.subject.keywordPlus | chemistry | - |
dc.subject.keywordPlus | differential scanning calorimetry | - |
dc.subject.keywordPlus | heat | - |
dc.subject.keywordPlus | infrared spectroscopy | - |
dc.subject.keywordPlus | protein secondary structure | - |
dc.subject.keywordPlus | X ray diffraction | - |
dc.subject.keywordPlus | Animals | - |
dc.subject.keywordPlus | Bombyx | - |
dc.subject.keywordPlus | Calorimetry, Differential Scanning | - |
dc.subject.keywordPlus | Carbon | - |
dc.subject.keywordPlus | Catalysis | - |
dc.subject.keywordPlus | Crystallization | - |
dc.subject.keywordPlus | Fibroins | - |
dc.subject.keywordPlus | Hot Temperature | - |
dc.subject.keywordPlus | Microscopy, Electron, Scanning | - |
dc.subject.keywordPlus | Protein Structure, Secondary | - |
dc.subject.keywordPlus | Silk | - |
dc.subject.keywordPlus | Spectroscopy, Fourier Transform Infrared | - |
dc.subject.keywordPlus | X-Ray Diffraction | - |
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