Study of melittin-membrane complex by time-resolved fluorescence spectroscopy
DOI:
https://doi.org/10.7124/bc.00009DAbstract
Structural dynamics of tetrameric melittin in solution and of the melittin-phospholipid membrane complex was studied by time-resolved fluorescence spoctroscopy. Significant differences in the spectral dependences of the mean tryptophan fluorescence lifetime of protein in solution and in the complex with liposomes were established.References
Talbot JC, Dufourcq J, de Bony J, Faucon JF, Lussan C. Conformational change and self association of monomeric melittin. FEBS Lett. 1979;102(1):191-3.
Demchenko AP, Kostrzhevskaia EG. Melittin: structure, properties, interaction with a membrane. Ukr Biokhim Zh. 1986;58(5):92-103.
Demchenko AP, Ladokhin AS, Kostrzhevskaia EG. Structural-dynamic properties of the tryptophan residue environment in melittin. Mol Biol (Mosk). 1987;21(3):663-71.
Kamalov VF, Razzhivin AP, Toleutaev BN, Chikishev AYu, Shkurinov AP. A laser subnanosecondfluorescent spectrometer with single photon counting. Kvantovaya elektronika. 1987, 14(6):1303-8.
Georghiou S, Thompson M, Mukhopadhyay AK. Melittin-phospholipid interaction studied by employing the single tryptophan residue as an intrinsic fluorescent probe. Biochim Biophys Acta. 1982;688(2):441-52.
Kamalov VF, Ladokhin AS, Toleutaev BN. Nanosecond intramolecular dynamics of melittin. Dokl Akad Nauk SSSR. 1987;296(3):742-5.
Ladokhin AS, Kostrezevskaya EG, Demchenko AP. Interaction of melittin with the phospholipid bilayer. "Surface" and "internal" protein forms. Doklady Akad Nauk Ukr SSR. Ser B. 1988; (11):65-7.
