Amphiphilic α-helices are important structural motifs in the a and β peptides that constitute the bacteriocin lactococcin G - Enhancement of helix formation upon α-β interaction

European Journal of Biochemistry

Volumn 251, Issue 3, 1998, Pages 565-572

  Hauge, Håvard Hildeng ^a   Nissen Meyer, Jon ^a   Nes, Ingolf F ^b   Eijsink, Vincent G H ^b  

^a UNIVERSITY OF OSLO   (Norway)

^b NORWEGIAN UNIVERSITY OF LIFE SCIENCES   (Norway)

Author keywords

Antimicrobial polypeptide; Bacteriocin; Circular dichroism; Lactococcin; Protein structure

Indexed keywords

DIOLEOYLPHOSPHATIDYLCHOLINE; DIOLEOYLPHOSPHATIDYLGLYCEROL; LACTOCOCCIN; LACTOCOCCIN A; LIPOSOME; TRIFLUOROETHANOL; UNCLASSIFIED DRUG;

ALPHA HELIX; AQUEOUS SOLUTION; ARTICLE; CIRCULAR DICHROISM; MICELLE; PRIORITY JOURNAL; PROTEIN PROTEIN INTERACTION;

BACTERIOCINS; CIRCULAR DICHROISM; MACROMOLECULAR SUBSTANCES; MICELLES; PHOSPHATIDYLGLYCEROLS; PHOSPHORYLCHOLINE; PROTEIN STRUCTURE, SECONDARY;

EID: 0032005933     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1327.1998.2510565.x     Document Type: Article

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