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Whilst rheology is the reference technique to study the mechanical properties of unspun silk, we know little of the structure and the dynamics that generate them. By coupling infrared spectroscopy and shearing forces to study silk fibroin conversion, we are introducing a novel tool to address this gap in our knowledge. Here the silk conversion process has been studied dynamically using polarized attenuated total reflectance Fourier transform infrared spectroscopy whilst applying shear, thus revealing silk protein conformation and molecular orientation in situ. Our results show that the silk conversion process starts with a pre-alignment of the proteins followed by a rapid growth of the β-sheet formation and then a subsequent deceleration of the growth. We propose that this tool will provide further insight into not only silk but any biopolymer solution, opening a new window into biological materials.

Original publication

DOI

10.1039/c0cp02599b

Type

Journal article

Journal

Phys Chem Chem Phys

Publication Date

07/03/2011

Volume

13

Pages

3979 - 3984

Keywords

Biopolymers, Fibroins, Protein Structure, Secondary, Spectroscopy, Fourier Transform Infrared