Abstract
In this work we analyzed the secondary structure of 13 globular proteins in KBr pellet through Fourier transform infrared spectroscopy (FTIR). The quantification was based in singular value decomposition (SVD) theory, a pattern recognition method. The results show better correlation for α helix (0.90) and β sheet (0.84) in amide I band, similar to the results obtained for proteins in solution. These results show that the protein secondary structure is conserved in solid state, in opposition to the results observed by FTIR using resolution enhancement techniques. The SVD analysis also show that in KBr pellets the protein secondary structures have absorbances in different wavenumbers when compared to those in solution. In this way, the use of KBr pellet and the pattern recognition method can be an ideal method to analyze protein secondary structure by FTIR.
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
