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A Robust Spectroscopic Method for the Determination of Protein Conformational Composition- Application to the Annealing of Silk.

Acta Biomaterialia(2018)

Cited 35|Views9
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Abstract
The physical and mechanical properties of structural proteins such as silk fibroin can be modified by controlled conformational change, which is regularly monitored by Fourier transform infrared spectroscopy by peak fitting of the amide I band envelope. Although many variables affecting peak shape are well established, there is no fixed methodology to compare and follow secondary structural differences without significant operator input especially where low frequency spectral noise is a problem.
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Key words
Silk,FTIR spectroscopy,Thioflavin T,Conformational change,Hydrogen bonding
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