Transmembrane Polyproline Helix.
J Phys Chem Lett
; 9(9): 2170-2174, 2018 May 03.
Article
em En
| MEDLINE
| ID: mdl-29638132
ABSTRACT
The third most abundant polypeptide conformation in nature, the polyproline-II helix, is a polar, extended secondary structure with a local organization stabilized by intercarbonyl interactions within the peptide chain. Here we design a hydrophobic polyproline-II helical peptide based on an oligomeric octahydroindole-2-carboxylic acid scaffold and demonstrate its transmembrane alignment in model lipid bilayers by means of solid-state 19F NMR. As result, we provide a first example of a purely artificial transmembrane peptide with a structural organization that is not based on hydrogen-bonding.
Texto completo:
1
Base de dados:
MEDLINE
Assunto principal:
Peptídeos
/
Ácidos Carboxílicos
/
Indóis
/
Proteínas de Membrana
Idioma:
En
Ano de publicação:
2018
Tipo de documento:
Article