(Q27658432)

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NMR Structure of Pardaxin, a Pore-forming Antimicrobial Peptide, in Lipopolysaccharide Micelles: MECHANISM OF OUTER MEMBRANE PERMEABILIZATION

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NMR Structure of Pardaxin, a Pore-forming Antimicrobial Peptide, in Lipopolysaccharide Micelles: MECHANISM OF OUTER MEMBRANE PERMEABILIZATION (English)

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lipopolysaccharide

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antimicrobial peptide

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based on heuristic

inferred from title

Ayyalusamy Ramamoorthy

5

object named as

Ayyalusamy Ramamoorthy

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author name string

Anirban Bhunia

1

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Prerna N Domadia

2

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Jaume Torres

3

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Kevin J Hallock

4

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Surajit Bhattacharjya

6

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language of work or name

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publication date

5 February 2010

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Journal of Biological Chemistry

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285

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6

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3883-95

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Helical hairpin structure of a potent antimicrobial peptide MSI-594 in lipopolysaccharide micelles by NMR spectroscopy

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High-resolution solution structure of a designed peptide bound to lipopolysaccharide: transferred nuclear Overhauser effects, micelle selectivity, and anti-endotoxic activity

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Lipopolysaccharide endotoxins

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Solution structure of pardaxin P-2.

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