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Título:
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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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Autores:
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Yélamos, Belén ;
Núñez, Elena ;
Gómez-Gutiérrez, Julián ;
Delgado, Carmen ;
Pacheco, Beatriz ;
Peterson, Darrell L. ;
Gavilanes, Francisco
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Tipo de documento:
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texto impreso
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Editorial:
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Elsevier Science BV, 2001-03-09
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Dimensiones:
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application/pdf
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Nota general:
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info:eu-repo/semantics/openAccess
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Idiomas:
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Palabras clave:
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Estado = Publicado
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Materia = Ciencias: Química: Bioquímica
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Tipo = Artículo
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Resumen:
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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.
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En línea:
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https://eprints.ucm.es/33611/1/Biochim.%20Biophys.%20Acta%201546%2C%2087-97%20%282001%29.pdf
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