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Volumn 132, Issue 51, 2010, Pages 18417-18428

Structure, interactions, and antibacterial activities of MSI-594 derived mutant peptide MSI-594F5A in lipopolysaccharide micelles: Role of the helical hairpin conformation in outer-membrane permeabilization

Author keywords

[No Author keywords available]

Indexed keywords

3D STRUCTURE; AMPHIPATHIC; ANTI-BACTERIAL ACTIVITY; ANTIMICROBIAL PEPTIDE; ATOMIC-RESOLUTION; BINDING AFFINITIES; CATIONIC ANTIMICROBIAL PEPTIDES; CYTOPLASMIC MEMBRANE; GAINING ACCESS; GRAM-NEGATIVE BACTERIA; GRAM-NEGATIVE PATHOGENS; HELICAL HAIRPINS; HELICAL SEGMENTS; HELICAL STRUCTURES; HOST DEFENSE; INNER MEMBRANES; INTERHELICAL INTERACTIONS; LIPOPOLYSACCHARIDES; MEMBRANE PERMEABILIZATION; NMR SPECTROSCOPY; OUTER MEMBRANE; PERMEABILITY BARRIERS; PERMEABILIZATION;

EID: 78650599747     PISSN: 00027863     EISSN: 15205126     Source Type: Journal    
DOI: 10.1021/ja1083255     Document Type: Article
Times cited : (104)

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* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.