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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...
Tallennettuna:
| Päätekijät: | , , , , , , , , , |
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| Aineistotyyppi: | Artigo |
| Kieli: | Inglês |
| Julkaistu: |
Biophysical Society
2006
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| Aiheet: | |
| Linkit: | 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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