A robust spectroscopic method for the determination of protein conformational composition - Application to the annealing of silk.

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. The aim of this contribution is to establish a method for such analyses to be carried at high levels of autonomy to prevent subjective or erroneous fitting. A range of approaches was trialled with optimal peak parameters selected based on overall goodness of fit and reproducibility of fit of replic

SUBMITTER: Belton DJ 

PROVIDER: S-EPMC5985223 | biostudies-literature | 2018 Jun

REPOSITORIES: biostudies-literature