Nanoscale probing of electron-regulated structural transitions in silk proteins by near-field IR imaging and nano-spectroscopy
Silk protein fibres produced by silkworms and spiders are renowned for their unparalleled mechanical strength and extensibility arising from their high-β-sheet crystal contents as natural materials. Investigation of β-sheet-oriented conformational transitions in silk proteins at the nanoscale remain...
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| Format: | Article |
| Language: | en_US |
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Nature Publishing Group
2017
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| Online Access: | http://hdl.handle.net/1721.1/109080 https://orcid.org/0000-0001-5311-6961 |
| _version_ | 1826194063343222784 |
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| author | Qin, Nan Zhang, Shaoqing Jiang, Jianjuan Corder, Stephanie Gilbert Qian, Zhigang Zhou, Zhitao Lee, Woonsoo Liu, Keyin Wang, Xiaohan Li, Xinxin Shi, Zhifeng Mao, Ying Bechtel, Hans A. Martin, Michael C. Xia, Xiaoxia Marelli, Benedetto Kaplan, David L. Omenetto, Fiorenzo G. Liu, Mengkun Tao, Tiger H. |
| author2 | Massachusetts Institute of Technology. Department of Civil and Environmental Engineering |
| author_facet | Massachusetts Institute of Technology. Department of Civil and Environmental Engineering Qin, Nan Zhang, Shaoqing Jiang, Jianjuan Corder, Stephanie Gilbert Qian, Zhigang Zhou, Zhitao Lee, Woonsoo Liu, Keyin Wang, Xiaohan Li, Xinxin Shi, Zhifeng Mao, Ying Bechtel, Hans A. Martin, Michael C. Xia, Xiaoxia Marelli, Benedetto Kaplan, David L. Omenetto, Fiorenzo G. Liu, Mengkun Tao, Tiger H. |
| author_sort | Qin, Nan |
| collection | MIT |
| description | Silk protein fibres produced by silkworms and spiders are renowned for their unparalleled mechanical strength and extensibility arising from their high-β-sheet crystal contents as natural materials. Investigation of β-sheet-oriented conformational transitions in silk proteins at the nanoscale remains a challenge using conventional imaging techniques given their limitations in chemical sensitivity or limited spatial resolution. Here, we report on electron-regulated nanoscale polymorphic transitions in silk proteins revealed by near-field infrared imaging and nano-spectroscopy at resolutions approaching the molecular level. The ability to locally probe nanoscale protein structural transitions combined with nanometre-precision electron-beam lithography offers us the capability to finely control the structure of silk proteins in two and three dimensions. Our work paves the way for unlocking essential nanoscopic protein structures and critical conditions for electron-induced conformational transitions, offering new rules to design protein-based nanoarchitectures. |
| first_indexed | 2024-09-23T09:49:56Z |
| format | Article |
| id | mit-1721.1/109080 |
| institution | Massachusetts Institute of Technology |
| language | en_US |
| last_indexed | 2024-09-23T09:49:56Z |
| publishDate | 2017 |
| publisher | Nature Publishing Group |
| record_format | dspace |
| spelling | mit-1721.1/1090802022-09-26T14:00:03Z Nanoscale probing of electron-regulated structural transitions in silk proteins by near-field IR imaging and nano-spectroscopy Qin, Nan Zhang, Shaoqing Jiang, Jianjuan Corder, Stephanie Gilbert Qian, Zhigang Zhou, Zhitao Lee, Woonsoo Liu, Keyin Wang, Xiaohan Li, Xinxin Shi, Zhifeng Mao, Ying Bechtel, Hans A. Martin, Michael C. Xia, Xiaoxia Marelli, Benedetto Kaplan, David L. Omenetto, Fiorenzo G. Liu, Mengkun Tao, Tiger H. Massachusetts Institute of Technology. Department of Civil and Environmental Engineering Marelli, Benedetto Silk protein fibres produced by silkworms and spiders are renowned for their unparalleled mechanical strength and extensibility arising from their high-β-sheet crystal contents as natural materials. Investigation of β-sheet-oriented conformational transitions in silk proteins at the nanoscale remains a challenge using conventional imaging techniques given their limitations in chemical sensitivity or limited spatial resolution. Here, we report on electron-regulated nanoscale polymorphic transitions in silk proteins revealed by near-field infrared imaging and nano-spectroscopy at resolutions approaching the molecular level. The ability to locally probe nanoscale protein structural transitions combined with nanometre-precision electron-beam lithography offers us the capability to finely control the structure of silk proteins in two and three dimensions. Our work paves the way for unlocking essential nanoscopic protein structures and critical conditions for electron-induced conformational transitions, offering new rules to design protein-based nanoarchitectures. National Science Foundation (U.S.) (1563422) National Science Foundation (U.S.) (1562915) 2017-05-15T14:25:56Z 2017-05-15T14:25:56Z 2016-10 2016-06 Article http://purl.org/eprint/type/JournalArticle 2041-1723 http://hdl.handle.net/1721.1/109080 Qin, Nan; Zhang, Shaoqing; Jiang, Jianjuan; Corder, Stephanie Gilbert; Qian, Zhigang; Zhou, Zhitao; Lee, Woonsoo et al. “Nanoscale Probing of Electron-Regulated Structural Transitions in Silk Proteins by Near-Field IR Imaging and Nano-Spectroscopy.” Nature Communications 7 (October 2016): 13079. © 2016 Macmillan Publishers Limited, part of Springer Nature https://orcid.org/0000-0001-5311-6961 en_US http://dx.doi.org/10.1038/ncomms13079 Nature Communications Creative Commons Attribution 4.0 International License http://creativecommons.org/licenses/by/4.0/ application/pdf Nature Publishing Group Nature |
| spellingShingle | Qin, Nan Zhang, Shaoqing Jiang, Jianjuan Corder, Stephanie Gilbert Qian, Zhigang Zhou, Zhitao Lee, Woonsoo Liu, Keyin Wang, Xiaohan Li, Xinxin Shi, Zhifeng Mao, Ying Bechtel, Hans A. Martin, Michael C. Xia, Xiaoxia Marelli, Benedetto Kaplan, David L. Omenetto, Fiorenzo G. Liu, Mengkun Tao, Tiger H. Nanoscale probing of electron-regulated structural transitions in silk proteins by near-field IR imaging and nano-spectroscopy |
| title | Nanoscale probing of electron-regulated structural transitions in silk proteins by near-field IR imaging and nano-spectroscopy |
| title_full | Nanoscale probing of electron-regulated structural transitions in silk proteins by near-field IR imaging and nano-spectroscopy |
| title_fullStr | Nanoscale probing of electron-regulated structural transitions in silk proteins by near-field IR imaging and nano-spectroscopy |
| title_full_unstemmed | Nanoscale probing of electron-regulated structural transitions in silk proteins by near-field IR imaging and nano-spectroscopy |
| title_short | Nanoscale probing of electron-regulated structural transitions in silk proteins by near-field IR imaging and nano-spectroscopy |
| title_sort | nanoscale probing of electron regulated structural transitions in silk proteins by near field ir imaging and nano spectroscopy |
| url | http://hdl.handle.net/1721.1/109080 https://orcid.org/0000-0001-5311-6961 |
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