2JX6
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![BU of 2jx6 by Molmil](/molmil-images/mine/2jx6) | Structure and membrane interactions of the antibiotic peptide dermadistinctin k by solution and oriented 15N and 31P solid-state NMR spectroscopy | 分子名称: | Dermadistinctin-K | 著者 | Mendonca Moraes, C, Verly, R.M, Resende, J.M, Bemquerer, M.P, Pilo-Veloso, D, Valente, A, Almeida, F.C.L, Bechinger, B. | 登録日 | 2007-11-08 | 公開日 | 2008-11-11 | 最終更新日 | 2022-03-16 | 実験手法 | SOLUTION NMR | 主引用文献 | Structure and membrane interactions of the antibiotic peptide dermadistinctin K by multidimensional solution and oriented 15N and 31P solid-state NMR spectroscopy Biophys.J., 96, 2009
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2JQ1
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![BU of 2jq1 by Molmil](/molmil-images/mine/2jq1) | Phylloseptin-3 | 分子名称: | Phylloseptin-3 | 著者 | Resende, J.M, Mendonca Moraes, C, Almeida, F.C.L, Prates, M.V, Cesar, A, Valente, A, Bemquerer, M.P, Pilo-Veloso, D, Bechinger, B. | 登録日 | 2007-05-25 | 公開日 | 2008-06-03 | 最終更新日 | 2023-12-20 | 実験手法 | SOLUTION NMR | 主引用文献 | Solution NMR structures of the antimicrobial peptides phylloseptin-1, -2, and -3 and biological activity: The role of charges and hydrogen bonding interactions in stabilizing helix conformations Peptides, 29, 2008
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2JQ0
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![BU of 2jq0 by Molmil](/molmil-images/mine/2jq0) | Phylloseptin-1 | 分子名称: | Phylloseptin-1 | 著者 | Resende, J.M, Mendonca Moraes, C, Almeida, F.C.L, Prates, M.V, Cesar, A, Valente, A, Bemquerer, M.P, Pilo-Veloso, D, Bechinger, B. | 登録日 | 2007-05-25 | 公開日 | 2008-06-03 | 最終更新日 | 2023-12-20 | 実験手法 | SOLUTION NMR | 主引用文献 | Solution NMR structures of the antimicrobial peptides phylloseptin-1, -2, and -3 and biological activity: The role of charges and hydrogen bonding interactions in stabilizing helix conformations Peptides, 29, 2008
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2JPY
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![BU of 2jpy by Molmil](/molmil-images/mine/2jpy) | Phylloseptin-2 | 分子名称: | Phylloseptin-2 protein | 著者 | Resende, J.M, Mendonca Moraes, C, Almeida, F.C.L, Prates, M.V, Cesar, A, Valente, A, Bemquerer, M.P, Pilo-Veloso, D, Bechinger, B. | 登録日 | 2007-05-24 | 公開日 | 2008-06-03 | 最終更新日 | 2023-12-20 | 実験手法 | SOLUTION NMR | 主引用文献 | Solution NMR structures of the antimicrobial peptides phylloseptin-1, -2, and -3 and biological activity: The role of charges and hydrogen bonding interactions in stabilizing helix conformations Peptides, 29, 2008
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