Partially Folded Conformations in the Folding Pathway of Bovine Carbonic Anhydrase II: A Fluorescence Spectroscopic Analysis

Autor:	Alexander G. Biktashev, Natalia A. Bushmarina, Vladimir N. Uversky, Konstantin K. Turoverov, Irina M. Kuznetsova
Rok vydání:	2001
Předmět:	biology Chemistry Carbonic anhydrase II Organic Chemistry Biochemistry Fluorescence Fluorescence spectroscopy Crystallography chemistry.chemical_compound Protein structure Carbonic anhydrase biology.protein Molecular Medicine Protein folding Guanidine Molecular Biology Fluorescence anisotropy
Zdroj:	ChemBioChem. 2:813
ISSN:	1439-7633 1439-4227
DOI:	10.1002/1439-7633(20011105)2:11<813::aid-cbic813>3.0.co;2-w
Popis:	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.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_________::5f04bd44cc034eff7cfa14b164a9c8a3 https://doi.org/10.1002/1439-7633(20011105)2:11<813::aid-cbic813>3.0.co Zobrazit plný text záznamu Plný text