Solution structure of trypsin modulating oostatic factor is a left-handed helix.
Biochem Biophys Res Commun
; 193(2): 688-93, 1993 Jun 15.
Article
em En
| MEDLINE
| ID: mdl-8512567
ABSTRACT
The solution structure of trypsin modulating oostatic factor (TMOF), a decapeptide (H-YDPAPPPPPP-OH) hormone that signals the termination of trypsin-like biosynthesis in mosquito midgut epithelial cells, was determined by 2-D 1H nuclear magnetic resonance spectroscopy and molecular modeling. The peptide forms a rod-shaped left-handed helix about 30 A long. No evidence was found to support a poly-L-proline beta-turn model. Hydrophobic contacts between the rings of tyrosine 1 and proline 3 may enhance the stability of the N-terminal segment. This peptide provides an interesting exception to the normal chemical shift index (csi) rules. Our results suggest that a sequence of positive csi indices, normally expected for a beta-strand structure, could also describe a left-handed poly-L-proline-like helix.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Oligopeptídeos
/
Estrutura Secundária de Proteína
Tipo de estudo:
Prognostic_studies
Idioma:
En
Revista:
Biochem Biophys Res Commun
Ano de publicação:
1993
Tipo de documento:
Article