Comparisons of Interfacial Phe, Tyr, and Trp Residues as Determinants of Orientation and Dynamics for GWALP Transmembrane Peptides

[Image: see text] Aromatic amino acids often flank the transmembrane alpha helices of integral membrane proteins. By favoring locations within the membrane–water interface of the lipid bilayer, aromatic residues Trp, Tyr, and sometimes Phe may serve as anchors to help stabilize a transmembrane orien...

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Detalles Bibliográficos
Autores principales: Sparks, Kelsey A., Gleason, Nicholas J., Gist, Renetra, Langston, Rebekah, Greathouse, Denise V., Koeppe, Roger E.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: American Chemical Society 2014
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4053069/
https://www.ncbi.nlm.nih.gov/pubmed/24829070
http://dx.doi.org/10.1021/bi500439x

Internet

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4053069/
https://www.ncbi.nlm.nih.gov/pubmed/24829070
http://dx.doi.org/10.1021/bi500439x

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