Abstract
We have previously investigated the time-resolved intensity and anisotropy decay of dansylated bovine serum albumin (BSA) using multifrequency phase and modulation fluorescence spectroscopy (J. Phys. Chem. 1993, 97, 4231-4238). The present study focuses on how protein denaturation affects the time-resolved fluorescence intensity and anisotropy decays. Specifically, we report results for the denaturation of BSA by urea and guanidine hydrochloride (Gd.HCl). The results demonstrate that the fluorescence intensity decay of dansylated BSA, native and denatured, is best described by a double exponential decay law. The short lifetime component reflects dansyl at the BSA exterior and the long component arises from dansyl located in a more hydrophobic environment
Sign-in/Register to access full text options 
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.
