The Role of Amphipathicity in the Folding, Self-association and Biological Activity of Multiple Subunit Small Proteins
Open Access
- 1 January 1995
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 270 (3) , 1048-1056
- https://doi.org/10.1074/jbc.270.3.1048
Abstract
No abstract availableKeywords
This publication has 46 references indexed in Scilit:
- The actions of melittin on membranesPublished by Elsevier ,2003
- Structural Basis of Amino Acid α Helix PropensityScience, 1993
- Similarities in melittin function group reactivities during self-association and association with lipid bilayersBiochemistry, 1992
- Thermodynamics of melittin tetramerization determined by circular dichroism and implications for protein foldingProtein Science, 1992
- Mechanism of the conformational transition of melittinBiochemistry, 1992
- A Thermodynamic Scale for the Helix-Forming Tendencies of the Commonly Occurring Amino AcidsScience, 1990
- Side Chain Contributions to the Stability of Alpha-Helical Structure in PeptidesScience, 1990
- General method for the rapid solid-phase synthesis of large numbers of peptides: specificity of antigen-antibody interaction at the level of individual amino acids.Proceedings of the National Academy of Sciences, 1985
- The structure of melittin. I. Structure determination and partial refinement.Journal of Biological Chemistry, 1982
- The structure of melittin in the form I crystals and its implication for melittin's lytic and surface activitiesBiophysical Journal, 1982