A noncovalent peptide complex as a model for an early folding intermediate of cytochrome c.
Biochemistry
; 32(38): 10271-6, 1993 Sep 28.
Article
en En
| MEDLINE
| ID: mdl-8399155
Horse heart cytochrome c is one of a small number of proteins for which the folding pathway has been elucidated in structural detail by pulsed hydrogen exchange and NMR. Those studies indicated that a partially folded intermediate with interacting N- and C-terminal helices is formed at an early stage of folding when most of the chain is still disordered. This report describes a peptide model for this early intermediate, consisting of a noncovalent complex between a heme-containing N-terminal fragment (residues 1-38) and a synthetic peptide corresponding to the C-terminal helix (residues 87-104). Far-UV circular dichroism and proton NMR indicate that the isolated peptides are largely disordered, but when combined, they form a flexible, yet tightly bound complex with enhanced helical structure. These results emphasize the importance of interactions between marginally stable elements of secondary structure in forming tertiary subdomains in protein folding.
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Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Péptidos
/
Estructura Secundaria de Proteína
/
Pliegue de Proteína
/
Grupo Citocromo c
Límite:
Animals
Idioma:
En
Revista:
Biochemistry
Año:
1993
Tipo del documento:
Article
Pais de publicación:
Estados Unidos