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	Provedor de dados BJMBR (2) Autor Winter,R. (2) Cordeiro,Y. (1) Kraineva,J. (1) Silva,J.L. (1) Vogtt,K. (1) Palavra-chave Aggregation (1) Co-solvents (1) High pressure (1) Hydrogen exchange nuclear magnetic resonance (1) Lysozyme (1) Pressure-assisted cold denaturation (1) Prion (1) Structural conversion (1) Mais... Tipo do documento Info:eu-repo/semantics/article (2) Ano 2005 (2) País Brazil (2) Idioma Inglês (2)		Ordenar por:  Relevância Autor Título Ano Registros recuperados: 2 Primeira ... 1 ... Última Volume and energy folding landscape of prion protein revealed by pressure BJMBR Cordeiro,Y.; Kraineva,J.; Winter,R.; Silva,J.L.. The main hypothesis for prion diseases proposes that the cellular protein (PrP C) can be altered into a misfolded, ß-sheet-rich isoform, the PrP Sc (from scrapie). The formation of this abnormal isoform then triggers the transmissible spongiform encephalopathies. Here, we discuss the use of high pressure as a tool to investigate this structural transition and to populate possible intermediates in the folding/unfolding pathway of the prion protein. The latest findings on the application of high pressure to the cellular prion protein and to the scrapie PrP forms will be summarized in this review, which focuses on the energetic and volumetric properties of prion folding and conversion. Tipo: Info:eu-repo/semantics/article Palavras-chave: Prion; High pressure; Structural conversion; Aggregation. Ano: 2005 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X2005000800006 Pressure-assisted cold denaturation of hen egg white lysozyme: the influence of co-solvents probed by hydrogen exchange nuclear magnetic resonance BJMBR Vogtt,K.; Winter,R.. COSY proton nuclear magnetic resonance was used to measure the exchange rates of amide protons of hen egg white lysozyme (HEWL) in the pressure-assisted cold-denatured state and in the heat-denatured state. After dissolving lysozyme in deuterium oxide buffer, labile protons exchange for deuterons in such a way that exposed protons are substituted rapidly, whereas "protected" protons within structured parts of the protein are substituted slowly. The exchange rates k obs were determined for HEWL under heat treatment (80ºC) and under high pressure conditions at low temperature (3.75 kbar, -13ºC). Moreover, the influence of co-solvents (sorbitol, urea) on the exchange rate was examined under pressure-assisted cold denaturation conditions, and the corresponding... Tipo: Info:eu-repo/semantics/article Palavras-chave: Pressure-assisted cold denaturation; Co-solvents; Lysozyme; Hydrogen exchange nuclear magnetic resonance. Ano: 2005 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X2005000800005 Registros recuperados: 2 Primeira ... 1 ... Última

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