Topology to geometry in protein folding: β-Lactoglobulin
Evolution of protein structure from random coil to native is first represented topologically by its time-dependent sequences of discretized Ramachandran basins occupied by successive backbone residues. Introducing energetic and entropic criteria at each instant of observation transforms the descript...
| Autores: | , , |
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| Tipo de recurso: | artículo |
| Estado: | Versión publicada |
| Fecha de publicación: | 2000 |
| País: | Argentina |
| Institución: | Consejo Nacional de Investigaciones Científicas y Técnicas |
| Repositorio: | CONICET Digital (CONICET) |
| Idioma: | inglés |
| OAI Identifier: | oai:ri.conicet.gov.ar:11336/78536 |
| Acceso en línea: | http://hdl.handle.net/11336/78536 |
| Access Level: | acceso abierto |
| Palabra clave: | Protein Folding Cooperativity https://purl.org/becyt/ford/1.6 https://purl.org/becyt/ford/1 |
| Sumario: | Evolution of protein structure from random coil to native is first represented topologically by its time-dependent sequences of discretized Ramachandran basins occupied by successive backbone residues. Introducing energetic and entropic criteria at each instant of observation transforms the description from a structurally ambiguous topological representation to an unambiguous geometric picture of the folding process. The method is applied with success to folding of β-lactoglobulin, traditionally perplexing because of its reputed nonhierarchical folding pattern. This molecule passes through a stage, ca. 0.1 μs duration, of transient, "flickering" α-helical structure, until a bit of tertiary structure forms that stabilizes the system long enough to allow it to pass to its native β-sheet. |
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