title: Partially folded conformations in the folding pathway of bovine carbonic anhydrase II: a fluorescence spectroscopic analysis.
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, I(lambda1) versus I(lambda2) dependence, where I(lambda1) and I(lambda2) are the fluorescence intensity values measured at wavelengths lambda(1) and lambda(2), respectively.
authors.affiliation: Institute of Cytology, Russian Academy of Sciences, Tikhoretsky Ave. 4, 194064 St. Petersburg, Russia.
authors.forename: N A
authors.initials: NA
authors.lastname: Bushmarina
authors.forename: I M
authors.initials: IM
authors.lastname: Kuznetsova
authors.forename: A G
authors.initials: AG
authors.lastname: Biktashev
authors.forename: K K
authors.initials: KK
authors.lastname: Turoverov
authors.forename: V N
authors.initials: VN
authors.lastname: Uversky
mesh_terms: D000818:Animals; D024402:Carbonic Anhydrase II / Q000737:chemistry* / Q000378:metabolism*; D002417:Cattle; D005454:Fluorescence Polarization; D019791:Guanidine / Q000494:pharmacology; D006863:Hydrogen-Ion Concentration; D011487:Protein Conformation / Q000187:drug effects; D011489:Protein Denaturation / Q000187:drug effects; D017510:Protein Folding; D020673:Protein Renaturation / Q000187:drug effects; D013050:Spectrometry, Fluorescence; D013997:Time Factors; D014508:Urea / Q000494:pharmacology
chemical_list: D014508:Urea; D024402:Carbonic Anhydrase II; D019791:Guanidine