Evaluation of protein secondary structure from FTIR spectra improved after partial deuteration.

ABSTRACT: FTIR spectroscopy has become a major tool to determine protein secondary structure. One of the identified obstacle for reaching better predictions is the strong overlap of bands assigned to different secondary structures. Yet, while for instance disordered structures and α-helical structures absorb almost at the same wavenumber, the absorbance bands are differentially shifted upon deuteration, in part because exchange is much faster for disordered structures. We recorded the FTIR spectra of 85 proteins at different stages of hydrogen/deuterium exchange process using protein microarrays and infrared imaging for high throughput measurements. Several methods were used to relate spectral shape to secondary structure content. While in absolute terms, β-sheet is always better predicted than α-he

SUBMITTER: De Meutter J 

PROVIDER: S-EPMC8189984 | biostudies-literature | 2021 May

REPOSITORIES: biostudies-literature