Stabilization of conformationally dynamic helices by covalently attached acyl chains
AUTOR(ES)
Poschner, Bernhard C
FONTE
Wiley Subscription Services
RESUMO
Acylation of proteins is known to mediate membrane attachment and to influence subcellular sorting. Here, we report that acylation can stabilize secondary structure. Circular dichroism spectroscopy showed that N-terminal attachment of acyl chains decreases the ability of an intrinsically flexible hydrophobic model peptide to refold from an α-helical state to β-sheet in response to changing solvent conditions. Acylation also stabilized the membrane-embedded α-helix. This increase of global helix stability did not result from decreased local conformational dynamics of the helix backbone as assessed by deuterium/hydrogen-exchange experiments. We concluded that acylation can stabilize the structure of intrinsically dynamic helices and may thus prevent misfolding.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=2776967Documentos Relacionados
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