Kinetics of conformational changes in melittin. A circular-dichroic stopped-flow study.
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.
D000838:Anions; D001514:Bee Venoms / Q000032:analysis*; D002942:Circular Dichroism; D003902:Detergents; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D008555:Melitten / Q000032:analysis*; D011487:Protein Conformation; D012996:Solutions
D000838:Anions; D001514:Bee Venoms; D003902:Detergents; D012996:Solutions; D008555:Melitten