Reversed-phase chromatography of synthetic amphipathic alpha-helical peptides as a model for ligand/receptor interactions. Effect of changing hydrophobic environment on the relative hydrophilicity/hydrophobicity of amino acid side-chains.

Abstract excerpt

To mimic a hydrophobic protein binding domain, which is a region on the surface of a protein that has a preference or a specificity to interact with a complementary surface, we have designed amphipathic alpha-helical peptides where the non-polar face interacts with the non-polar surface of a reve...

Topics

• Alanine
• Amino Acid Sequence
• Amino Acids
• Chemical Phenomena
• Chemistry, Physical
• Chromatography, High Pressure Liquid
• Computer Simulation
• Hydrogen-Ion Concentration
• Leucine
• Ligands
• Models, Chemical
• Molecular Sequence Data
• Mutation
• Peptides