Redesigning Channel-Forming Peptides: Amino Acid Substitutions that Enhance Rates of Supramolecular Self-Assembly and Raise Ion Transport Activity

Three series of 22-residue peptides derived from the transmembrane M2 segment of the glycine receptor α1-subunit (M2GlyR) have been designed, synthesized, and tested to determine the plasticity of a channel-forming sequence and to define whether channel pores with enhanced conductive properties coul...

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Detalhes bibliográficos
Main Authors: Shank, Lalida P., Broughman, James R., Takeguchi, Wade, Cook, Gabriel, Robbins, Ashley S., Hahn, Lindsey, Radke, Gary, Iwamoto, Takeo, Schultz, Bruce D., Tomich, John M.
Formato: Artigo
Idioma:Inglês
Publicado em: Biophysical Society 2006
Assuntos:
Supramolecular Assemblies
Acesso em linha:https://ncbi.nlm.nih.gov/pmc/articles/PMC1386792/
https://ncbi.nlm.nih.gov/pubmed/16387776
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1529/biophysj.105.070078
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