%0 Journal Article
%A Yélamos, Belén
%A Núñez, Elena
%A Gómez-Gutiérrez, Julián
%A Delgado, Carmen
%A Pacheco, Beatriz
%A Peterson, Darrell L.
%A Gavilanes, Francisco
%T Urea equilibrium unfolding of the major core protein of the  retrovirus feline immunodeficiency virus and its tryptophan  mutants
%D 2001
%@ 0167-4838
%U https://hdl.handle.net/20.500.14352/59749
%X Circular dichroism and fluorescence spectroscopy have been employed to study the urea unfolding mechanism of a recombinant form of the major core protein of feline immunodeficiency virus (FIV-rp24) and its native tryptophan mutants. The equilibrium denaturation curves indicate the existence of two transitions. The first unfolding transition most likely reflects the denaturation of the carboxy-terminal region of FIV-rp24. Consequently, the second transition, where the changes in fluorescence are produced, should reflect the denaturation of the amino-terminal region. If the intermediate observed upon urea denaturation is an on- pathway species, the data described herein can reflect the sequential and independent loss of structure of the two domains that this type of proteins possesses.
%~