Myoglobin forms amyloid fibrils by association of unfolded polypeptide segments.
Proc Natl Acad Sci U S A
; 100(26): 15463-8, 2003 Dec 23.
Article
em En
| MEDLINE
| ID: mdl-14665689
ABSTRACT
Observations that beta-sheet proteins form amyloid fibrils under at least partially denaturing conditions has raised questions as to whether these fibrils assemble by docking of preformed beta-structure or by association of unfolded polypeptide segments. By using alpha-helical protein apomyoglobin, we show that the ease of fibril assembly correlates with the extent of denaturation. By contrast, monomeric beta-sheet intermediates could not be observed under the conditions of fibril formation. These data suggest that amyloid fibril formation from apomyoglobin depends on disordered polypeptide segments and conditions that are selectively unfavorable to folding. However, it is inevitable that such conditions often stabilize protein folding intermediates.
Texto completo:
1
Base de dados:
MEDLINE
Assunto principal:
Peptídeos
/
Miofibrilas
/
Mioglobina
Tipo de estudo:
Risk_factors_studies
Limite:
Animals
Idioma:
En
Ano de publicação:
2003
Tipo de documento:
Article