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January 2, 1989FEBS Letters

Short model peptides having a high α‐helical tendency: Design and solution properties

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Authors

JKJohn L. KrstenanskyKeck Graduate InstituteTOThomas J. OwenRichland CollegeKHKaren A. HagamanIndiana Wesleyan University

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Cite This Study

Krstenansky et al. (1989) studied this question.

synapsesocial.com/papers/6a90d47a152a692a9d92cb9fhttps://doi.org/10.1016/0014-5793(89)80512-5
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Also Consider

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

  1. 1Studies of synthetic peptide analogs of the amphipathic helix. Effect of charged amino acid residue topography on lipid affinity.1980 · 92 citations
  2. 2Interaction of a synthetic amphiphilic polypeptide and lipids in a bilayer structure1983 · 111 citations
  3. 3A synthetic amphiphilic helical docosapeptide with the surface properties of plasma apolipoprotein A-I1979 · 76 citations
  4. 4Nature of the charged-group effect on the stability of the C-peptide helix.1985 · 314 citations
  5. 5Studies of synthetic peptide analogs of the amphipathic helix. Effect of charge distribution, hydrophobicity, and secondary structure on lipid association and lecithin:cholesterol acyltransferase activation.1987 · 82 citations