Kinetics of conformational changes in melittin. A circular-dichroic stopped-flow studyududEur J Biochem. 1984 Mar 1;139(2):275-8.

摘要

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.