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Two-dimensional 1H NMR experiments show that the 23-residue magainin antibiotic peptide is an α-helix in dodecylphosphocholine micelles, sodium dodecylsulfate micelles, and trifluoroethanol/water solution

Gesell, Jennifer, Zasloff, Michael, Opella, Stanley J.·1997·Journal of Biomolecular NMR
DOI 10.1023/a:1018698002314
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Metadata

Authors
Gesell, J., Zasloff, M., & Opella, S. J.
Venue
Journal of Biomolecular NMR
Publisher
Springer Science and Business Media LLC
Published
1997-02
Volume
9
Issue
2
Pages
127-135
ISSN
  • 0925-2738 (ISSN-L)
  • 1573-5001
DOI
10.1023/a:1018698002314
OpenAlex
W1945664147
Cited by
274
References
0
FWCI
3.26
Type
journal article
Language
en
Open access
closed
Licence

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CoChat. (2026). Citation check: Two-dimensional 1H NMR experiments show that the 23-residue magainin antibiotic peptide is an α-helix in dodecylphosphocholine micelles, sodium dodecylsulfate micelles, and trifluoroethanol/water solution. https://app.cochat.ai/papers/10.1023/a:1018698002314
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Gesell, J., Zasloff, M., & Opella, S. J. (1997). Two-dimensional 1H NMR experiments show that the 23-residue magainin antibiotic peptide is an α-helix in dodecylphosphocholine micelles, sodium dodecylsulfate micelles, and trifluoroethanol/water solution. Journal of Biomolecular NMR. https://doi.org/10.1023/a%3A1018698002314

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