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.
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.
Author(s): RESENDE, J. M.; MORAES, C. M.; PRATES, M. V.; CESAR, A.; ALMEIDA, F. C. L.; MUNDIM, N. C. C. R.; VALENTE, A. P.; BEMQUEREE, M. P.; PILO VELOSO, D.; BECHINGER, B.
Publication year: 2008
Types of publication: Journal article
Keywords: Peptídeo, Phyllomedusa, Rã
Observation
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