Proline-induced disruption of a transmembrane alpha-helix in its natural environment.
J Mol Biol
; 284(4): 1165-75, 1998 Dec 11.
Article
en En
| MEDLINE
| ID: mdl-9837734
ABSTRACT
alpha-Helix formation in globular proteins has been studied both theoretically and experimentally for decades, while a lack of both high-resolution structures and suitable experimental techniques has hampered the study of helices in membrane proteins. We have developed a new experimental approach, glycosylation mapping, where the active site of the lumenally exposed endoplasmic reticulum enzyme oligosaccharyl transferase is used as a point of reference against which the position of a transmembrane segment in the membrane can be measured. Here, we report an initial analysis of the helix-breaking properties of proline residues inserted in a transmembrane helix. We find that proline residues can break a transmembrane helix, but only when inserted near the end, and only when the helix is sufficiently long. The glycosylation mapping technique may be generally useful for determining the position of transmembrane helices in the membrane.
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Banco de datos:
MEDLINE
Asunto principal:
Prolina
/
Hexosiltransferasas
/
Proteínas de la Membrana
Idioma:
En
Año:
1998
Tipo del documento:
Article