Kinetics of conformational changes in melittin. A circular-dichroic stopped-flow study
- 1 March 1984
- journal article
- research article
- Published by Wiley in European Journal of Biochemistry
- Vol. 139 (2) , 275-278
- https://doi.org/10.1111/j.1432-1033.1984.tb08004.x
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 have aggregated into a polymeric assembly. Interaction with detergent micelles followed more complex kinetics.This publication has 11 references indexed in Scilit:
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