Folding of a pressure-denatured model protein

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The noncovalent complex formed by the association of two fragments of chymotrypsin inhibitor-2 is reversibly denatured by pressure in the absence of chemical denaturants. On pressure release, the complex returned to its original conformation through a biphasic reaction, with first-order rate constan...

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Detalles Bibliográficos
Autores principales:	Mohana-Borges, R., Silva, J.L., Ruiz-Sanz, J., De Prat-Gay, G.
Formato:	JOUR
Materias:	article atmospheric pressure chemical reaction kinetics concentration response mathematical analysis priority journal protein conformation protein denaturation protein folding temperature dependence Kinetics Models, Chemical Peptides Plant Proteins Pressure Protein Denaturation Protein Folding Serine Proteinase Inhibitors Temperature Thermodynamics
Acceso en línea:	http://hdl.handle.net/20.500.12110/paper_00278424_v96_n14_p7888_MohanaBorges
Aporte de:	Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires

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