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
Observation
Some of Embrapa's publications are published as ePub files. To read them, use or download one of the following free software options to your computer or mobile device. Android: Google Play Books; IOS: iBooks; Windows and Linux: Calibre.
Access other publications
Access the Agricultural Research Database (BDPA) to consult Embrapa's full library collection and records.
Visit Embrapa Bookstore to purchase books and other publications sold by Embrapa.