Cargando…
Illuminating Disorder Induced by Glu in a Stable Arg-Anchored Transmembrane Helix
[Image: see text] Membrane proteins are vital for biological function and are complex to study. Even in model peptide-lipid systems, the combined influence or interaction of pairs of chemical groups still is not well understood. Disordered proteins, whether in solution or near lipid membranes, are a...
Autores principales: | Price, Jake R., Afrose, Fahmida, Greathouse, Denise V., Koeppe, Roger E. |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
American Chemical Society
2021
|
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8359125/ https://www.ncbi.nlm.nih.gov/pubmed/34396006 http://dx.doi.org/10.1021/acsomega.1c02800 |
Ejemplares similares
-
Comparing Interfacial Trp, Interfacial His and pH Dependence for the Anchoring of Tilted Transmembrane Helical Peptides
por: Afrose, Fahmida, et al.
Publicado: (2020) -
Influence of High pH and Cholesterol on Single Arginine-Containing
Transmembrane Peptide Helices
por: Thibado, Jordana K., et al.
Publicado: (2016) -
Comparisons of Interfacial Phe, Tyr, and Trp Residues
as Determinants of Orientation and Dynamics for GWALP Transmembrane
Peptides
por: Sparks, Kelsey A., et al.
Publicado: (2014) -
Lipid-Dependent Titration of Glutamic Acid at a Bilayer
Membrane Interface
por: McKay, Matthew J., et al.
Publicado: (2021) -
Transmembrane helix: simple or complex
por: Wong, Wing-Cheong, et al.
Publicado: (2012)