+Search query
-Structure paper
Title | High-resolution structures and orientations of antimicrobial peptides piscidin 1 and piscidin 3 in fluid bilayers reveal tilting, kinking, and bilayer immersion. |
---|---|
Journal, issue, pages | J. Am. Chem. Soc., Vol. 136, Page 3491-3504, Year 2014 |
Publish date | Aug 27, 2013 (structure data deposition date) |
Authors | Perrin, B.S. / Tian, Y. / Fu, R. / Grant, C.V. / Chekmenev, E.Y. / Wieczorek, W.E. / Dao, A.E. / Hayden, R.M. / Burzynski, C.M. / Venable, R.M. ...Perrin, B.S. / Tian, Y. / Fu, R. / Grant, C.V. / Chekmenev, E.Y. / Wieczorek, W.E. / Dao, A.E. / Hayden, R.M. / Burzynski, C.M. / Venable, R.M. / Sharma, M. / Opella, S.J. / Pastor, R.W. / Cotten, M.L. |
External links | J. Am. Chem. Soc. / PubMed:24410116 |
Methods | NMR (solid-state) |
Structure data | PDB-2mcu: PDB-2mcv: PDB-2mcw: PDB-2mcx: |
Source |
|
Keywords | ANTIMICROBIAL PROTEIN / antimicrobial peptide / anticancer peptide / anti HIV-1 / cationic / amphipathic / histidine rich / helical / lipid bilayers / bacterial cell membrane mimic |