| dc.creator | Ferreira, Sérgio T. | |
| dc.creator | De Felice, Fernanda G. | |
| dc.creator | Chapeaurouge, Alexander | |
| dc.date | 2020-01-16T15:03:38Z | |
| dc.date | 2020-01-16T15:03:38Z | |
| dc.date | 2006 | |
| dc.date.accessioned | 2023-09-26T22:41:09Z | |
| dc.date.available | 2023-09-26T22:41:09Z | |
| dc.identifier | FERREIRA, Sérgio T.; DE FELICE, Fernanda G.; CHAPEUAROUGE, Alexander. Metastable, Partially Folded States in the Productive Folding and in the Misfolding and Amyloid Aggregation of Proteins. Cell Biochemistry and Biophysics, v. 44, p. 539-548. 2006. | |
| dc.identifier | 1085-9195 | |
| dc.identifier | https://www.arca.fiocruz.br/handle/icict/39268 | |
| dc.identifier | 10.1385/CBB:44:3:539 | |
| dc.identifier | 1559-0283 | |
| dc.identifier.uri | https://repositorioslatinoamericanos.uchile.cl/handle/2250/8881919 | |
| dc.description | Understanding the energetic and structural basis of protein folding in a physiological context may represent
an important step toward the elucidation of protein misfolding and aggregation events that take place in several
pathological states. In particular, investigation of the structure and thermodynamic properties of partially folded
intermediate states involved in productive folding or in misfolding/aggregation may provide insight into these
processes and suggest novel approaches to prevent misfolding in living organisms. This goal, however, has
remained elusive, because such intermediates are often transient and correspond to metastable states that are little
populated under physiological conditions. Characterization of these states requires their stabilization by
means of manipulation of the experimental conditions, involving changes in temperature, pH, or addition of different
types of denaturants. In the past few years, hydrostatic pressure has been increasingly used as a thermodynamic
variable in the study of both protein folding and misfolding/aggregation transitions. Compared with
other chemical or physical denaturing agents, a unique feature of pressure is its ability to induce subtle changes
in protein conformation, allowing the stabilization of partially folded states that are usually not significantly
populated under more drastic conditions. Much of the recent work in this field has focused on the characterization
of folding intermediates, because they seem to be involved in a variety of disease-causing protein misfolding
and aggregation reactions. Here, we review recent examples of the use of hydrostatic pressure as a tool to
gain insight into the forces and energetics governing the productive folding or the misfolding and amyloid
aggregation of proteins. | |
| dc.description | 2022-01-01 | |
| dc.format | application/pdf | |
| dc.language | eng | |
| dc.publisher | Springer | |
| dc.rights | restricted access | |
| dc.subject | Dobramento de proteínas | |
| dc.subject | Pressão hidrostática | |
| dc.subject | Agregados amilóides | |
| dc.subject | Desempenho | |
| dc.subject | Protein folding | |
| dc.subject | Misfolding | |
| dc.subject | Amyloid aggregates | |
| dc.subject | Hydrostatic pressure | |
| dc.title | Metastable, Partially Folded States in the Productive Folding and in the Misfolding and Amyloid Aggregation of Proteins | |
| dc.type | Article | |
