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Effects of Lys to Glu mutations in GsMTx4 on membrane binding, peptide orientation, and self-association propensity, as analyzed by molecular dynamics simulations
GsMTx4, a gating modifier peptide acting on cationic mechanosensitive channels, has a positive charge (+5 e) due to six Lys residues. The peptide does not have a stereospecific binding site on the channel but acts from the boundary lipids within a Debye length of the pore probably by changing local...
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| Vydáno v: | Biochim Biophys Acta |
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| Hlavní autoři: | , , , , , |
| Médium: | Artigo |
| Jazyk: | Inglês |
| Vydáno: |
2015
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| Témata: | |
| On-line přístup: | https://ncbi.nlm.nih.gov/pmc/articles/PMC4598310/ https://ncbi.nlm.nih.gov/pubmed/26342676 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1016/j.bbamem.2015.09.003 |
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