Noncovalent immobilized artificial membrane chromatography, an improved method for describing peptide–lipid bilayer interactions
Author:
Publisher
Elsevier BV
Subject
Organic Chemistry,General Medicine,Biochemistry,Analytical Chemistry
Reference28 articles.
1. The nature of the hydrophobic binding of small peptides at the bilayer interface: implications for the insertion of transbilayer helices
2. Electrostatic and nonpolar peptide-membrane interactions. Lipid binding and functional properties of somatostatin analogs of charge z = +1 to z = +3
3. Quantitation of Electrostatic and Hydrophobic Membrane Interactions by Equilibrium Dialysis and Reverse-Phase HPLC
4. Amphiphilic Secondary Structure: Design of Peptide Hormones
5. A method for probing the affinity of peptides for amphiphilic surfaces
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