Stabilization of partially folded states in protein folding/misfolding transitions by hydrostatic pressure

dc.creatorFerreira, S. T.
dc.creatorChapeaurouge, A.
dc.creatorDe Felice, F. G.
dc.date2019-12-07T14:30:06Z
dc.date2019-12-07T14:30:06Z
dc.date2005
dc.date.accessioned2023-09-26T22:52:25Z
dc.date.available2023-09-26T22:52:25Z
dc.identifierFERREIRA, S. T.; CHAPEAUROUGE, A.; DE FELICE, F. G. de. Stabilization of partially folded states in protein folding/misfolding transitions by hydrostatic pressure. Brazilian Journal of Medical and Biological Research, Ribeirão Preto, v. 38, n. 8, p. 1215-1222, 2005.
dc.identifier0100-879X
dc.identifierhttps://www.arca.fiocruz.br/handle/icict/37699
dc.identifier10.1590/s0100-879x2005000800009
dc.identifier1414-431X
dc.identifier.urihttps://repositorioslatinoamericanos.uchile.cl/handle/2250/8884220
dc.descriptionIn the last few years, hydrostatic pressure has been extensively used in the study of both protein folding and misfolding/aggregation. Compared to other chemical or physical denaturing agents, a unique feature of pressure is its ability to induce subtle changes in protein conformation, which allow the stabilization of partially folded intermediate states that are usually not significantly populated under more drastic conditions (e.g., in the presence of chemical denaturants or at high temperatures). Much of the recent research in the field of protein folding has focused on the characterization of folding intermediates since these species appear to be involved in a variety of disease-causing protein misfolding and aggregation events. The exact mechanisms of these biological phenomena, however, are still poorly understood. Here, we review recent examples of the use of hydrostatic pressure as a tool to obtain insight into the forces and energetics governing the productive folding or the misfolding and aggregation of proteins.
dc.formatapplication/pdf
dc.languageeng
dc.publisherAssociação Brasileira de Divulgação Científica
dc.rightsopen access
dc.subjectAlta pressão
dc.subjectDobramento de proteínas
dc.subjectAmilóide
dc.subjectAgregação
dc.subjectDeficiências na Proteostase
dc.subjectHigh pressure
dc.subjectProtein folding
dc.subjectMisfolding
dc.subjectAmyloid
dc.subjectAggregation
dc.titleStabilization of partially folded states in protein folding/misfolding transitions by hydrostatic pressure
dc.typeArticle


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