The topology of lysine-containing amphipathic peptides in bilayers by circular dichroism, solid-state NMR, and molecular modeling

Biophysical Journal

Volumn 79, Issue 5, 2000, Pages 2644-2656

  Vogt, Bas ^a   Ducarme, Philippe ^b   Schinzel, Susan ^a   Brasseur, Robert ^b   Bechinger, Burkhard ^a  

^a MAX PLANCK INSTITUTE OF BIOCHEMISTRY   (Germany)

^b UNIVERSITY OF LIÈGE   (Belgium)

Author keywords

[No Author keywords available]

Indexed keywords

LYSINE;

ALPHA HELIX; ARTICLE; BILAYER MEMBRANE; CIRCULAR DICHROISM; HYDROGEN BOND; HYDROPHOBICITY; MOLECULAR MODEL; NONHUMAN; PEPTIDE SYNTHESIS; PHOSPHOLIPID MEMBRANE; PHOSPHORUS NUCLEAR MAGNETIC RESONANCE; PROTEIN ASSEMBLY; PROTEIN CONFORMATION; PROTEIN SECONDARY STRUCTURE; SOLID STATE;

EID: 0033737012     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(00)76503-9     Document Type: Article

References (5)

1. Bechinger, B. 1996. Towards membrane protein design: pH dependent topology of histidine-containing polypeptides. J. Mol. Biol. 263: 768-775.
2. Bechinger, B. 1997. Structure and functions of channel-forming polypeptides: magainins, cecropins, melittin and alamethicin. J. Membr. Biol. 156:197-211.
3. Bechinger, B. 1999. The structure, dynamics and orientation of antimicrobial peptides in membranes by solid-state NMR spectroscopy. Biochim. Biophys. Acta. 1462:157-183.
4. Bechinger, B. 2000. Biophysical investigations of membrane perturbations by polypeptides using solid-state NMR spectroscopy. Mol. Membr. Biol. in press.
5. Zhang, Y. P., R. N. Lewis, G. D. Henry, B. D. Sykes, R. S. Hodges, and R. N. McElhaney. 1995. Peptide models of helical hydrophobic transmembrane segments of membrane proteins. 1. Studies of the conformation, intrabilayer orientation, and amide hydrogen exchangeability of Ac-K2-(LA)12-K2-amide. Biochemistry. 34:2348-2361.