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Urea equilibrium unfolding of the major core protein of the retrovirus feline immunodeficiency virus and its tryptophan mutants

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Yélamos, Belén and Núñez, Elena and Gómez-Gutiérrez, Julián and Delgado, Carmen and Pacheco, Beatriz and Peterson, Darrell L. and Gavilanes, Francisco (2001) Urea equilibrium unfolding of the major core protein of the retrovirus feline immunodeficiency virus and its tryptophan mutants. Biochimica et Biophysica Acta - Protein Structure and Molecular Enzymology, 1546 (1). pp. 87-97. ISSN 0167-4838

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Official URL: http://www.sciencedirect.com/science/article/pii/S0167483800003009



Abstract

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.


Item Type:Article
Uncontrolled Keywords:FIV core protein; tryptophan mutants; site-directed mutagenesis; urea denaturation; folding intermediates
Subjects:Sciences > Chemistry > Biochemistry
ID Code:33611
Deposited On:16 Oct 2015 08:03
Last Modified:16 Oct 2015 12:25

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