Kinetics of conformational changes in melittin: A circular‐dichroic stopped‐flow study

Abstract

The kinetics of the conformational changes undergone by melittin in aqueous solution upon interaction with ions and/or detergents were studied by following the variations of intrinsic ellipticity of the peptide with a circular‐dichroic stopped‐flow apparatus. The results were consistent with a simplified model in which salt induces a modification of the structure of melittin monomer, which may then aggregate into a polymeric assembly. Interaction with detergent micelles followed more complex kinetics. Copyright © 1984, Wiley Blackwell. All rights reserved