Partially Folded Conformations in The Folding Pathway of Bovine Carbonic Anhydrase II: A Fluorescence Spectroscopic Analysis
Document Type
Article
Publication Date
2001
Digital Object Identifier (DOI)
https://doi.org/10.1002/1439-7633(20011105)2:11%3C813::AID-CBIC813%3E3.0.CO;2-W
Abstract
GdmCl-, urea-, and pH-induced unfolding pathways of bovine carbonic anhydrase II have been analyzed by using changes induced by different denaturing agents in intensity, anisotropy, life time, and parameter A value of intrinsic fluorescence as well as intensity and life time of ANS (ammonium salt of 8-anilinonaphthalene-1-sulfonic acid) fluorescence. The formation of several stable unfolding intermediates, some of which were not observed previously, has been established. This was further confirmed by representation of fluorescence data in terms of a “phase diagram”, that is, Iλ1 versus Iλ2 dependence, where Iλ1 and Iλ2 are the fluorescence intensity values measured at wavelengths λ1 and λ2, respectively.
Was this content written or created while at USF?
Yes
Citation / Publisher Attribution
ChemBioChem, v. 2, issue 11, p. 813-821
Scholar Commons Citation
Bushmarina, Natalia A.; Kuznetsova, Irina M.; Biktashev, Alexander G.; Turoverov, Konstantin K.; and Uversky, Vladimir N., "Partially Folded Conformations in The Folding Pathway of Bovine Carbonic Anhydrase II: A Fluorescence Spectroscopic Analysis" (2001). Molecular Medicine Faculty Publications. 675.
https://digitalcommons.usf.edu/mme_facpub/675
