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August 1, 1998Journal of Peptide Research

Influence of preformed α‐helix and α‐helix induction on the activity of cationic antimicrobial peptides

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Authors

MHMichael E. HoustonCarolinas Medical CenterLKLeslie H. KondejewskiUniversity of AlbertaDKD. Nedra KarunaratneUniversity of Peradeniya

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Cite This Study

Houston et al. (1998) studied this question.

synapsesocial.com/papers/6a76eeeb3da069e66cbd6df6https://doi.org/10.1111/j.1399-3011.1998.tb01361.x
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Also Consider

Synapse has enriched 5 closely related papers on similar clinical questions. Consider them for comparative context:

  1. 1Helix stabilization by Glu-...Lys+ salt bridges in short peptides of de novo design.1987 · 962 citations
  2. 2Use of the fluorescent probe 1-N-phenylnaphthylamine to study the interactions of aminoglycoside antibiotics with the outer membrane of Pseudomonas aeruginosa1984 · 493 citations
  3. 3Determination of the helix and β form of proteins in aqueous solution by circular dichroism1974 · 2,069 citations
  4. 4Improvement of outer membrane-permeabilizing and lipopolysaccharide-binding activities of an antimicrobial cationic peptide by C-terminal modification1994 · 168 citations
  5. 5Lactam bridge stabilization of α‐helical peptides: Ring size, orientation and positional effects1995 · 81 citations