Abstract
Thermal denaturation of ribonuclease A (RNase A) in D 2O solution is studied by Fourier transform infrared (FT-IR) spectroscopy. Sample–sample two-dimensional correlation (SS 2D) spectroscopy and principal component analysis (PCA) are applied to these spectral data to reveal the thermal kinetics of RNase A. The second scores plot of PCA constructed from temperature-dependent original IR spectra illustrates a pretransition at 46 °C as well as a clear main transition at 66 °C. The latter is revealed by the SS 2D correlation spectra and the first score of PCA because of their illustration of the main denaturation event of RNase A, while the former cannot. Therefore, the present study demonstrates the great potential of PCA in revealing subtle phase transition of proteins in aqueous solutions.
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.
