Artículos
Título:
Role for the alpha-Helix in Aberrant Protein Aggregation
Autor/es:
RANI KUNJITHAPATHAM; FABIANA Y. OLIVA; URMI DOSHI; MAR PÉREZ; JESUS Á VILA; VICTOR MUÑOZ
Editorial:
American Chemical Society
Referencias:
Lugar: USA; Año: 2005 vol. 44 p. 149 - 149
Resumen:
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Is the alpha-helix structure capable of triggering the formation of aberrant protein aggregates? To answer this question, we investigate the in Vitro aggregation of tau protein in the presence of the helix inducing agent TFE. Tau is a natively unfolded protein that binds to microtubules and forms aggregates in Alzheimer?s disease. We find that full-length tau has residual alpha-helix structure, which is further enhanced by three mutations involved in genetic neurological disorders. TFE concentrations matching an alpha