Nanoscale probing of electron-regulated structural transitions in silk proteins by near-field IR imaging and nano-spectroscopy
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Nanoscale probing.pdf
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1.77 MB
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Checksum (MD5)
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Author(s)
Qin, Nan
Zhang, Shaoqing
Jiang, Jianjuan
Corder, Stephanie Gilbert
Qian, Zhigang
Zhou, Zhitao
Lee, Woonsoo
Liu, Keyin
Wang, Xiaohan
Li, Xinxin
Date Issued
October 2016
Journal
Nature Communications
Publisher
Nature Publishing Group
Citation
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
Version
Final published version
Abstract
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.
MIT Department
Massachusetts Institute of Technology. Department of Civil and Environmental Engineering
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Creative Commons Attribution 4.0 International License
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DOI of Published Version
https://doi.org/10.1038/ncomms13079
