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Partially Folded Conformations in the Folding Pathway of Bovine Carbonic Anhydrase II: A Fluorescence Spectroscopic Analysis
Author(s) -
Bushmaritalia A.,
Kuznetsova Irina M.,
Biktashev Alexander G.,
Turoverov Konstantin K.,
Uversky Vladimir N.
Publication year - 2001
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/1439-7633(20011105)2:11<813::aid-cbic813>3.0.co;2-w
Subject(s) - fluorescence , carbonic anhydrase , chemistry , carbonic anhydrase ii , protein folding , fluorescence anisotropy , crystallography , folding (dsp implementation) , enzyme , biochemistry , physics , quantum mechanics , membrane , electrical engineering , engineering
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 λ 1 versus I λ 2 dependence, where I λ 1 and I λ 2 are the fluorescence intensity values measured at wavelengths λ 1 and λ 2 , respectively.