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.
Kinetics of conformational changes in melittin. A circular-dichroic stopped-flow study Eur J Biochem. 1984 Mar 1;139(2):275-8 / Salerno, Costantino; Crifo', Carlo; Strom, Roberto. - In: EUROPEAN JOURNAL OF BIOCHEMISTRY. - ISSN 0014-2956. - STAMPA. - 139:2(1984), pp. 275-278. [10.1111/j.1432-1033.1984.tb08004.x]
Kinetics of conformational changes in melittin. A circular-dichroic stopped-flow study Eur J Biochem. 1984 Mar 1;139(2):275-8.
SALERNO, Costantino;CRIFO', Carlo;STROM, Roberto
1984
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.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
