Thermodynamics of melittin binding to lipid bilayers. Aggregation and pore formation.

Volume: 48, Issue: 12, Pages: 2586 - 2596
Published: Mar 31, 2009
Abstract
Lipid membranes act as catalysts for protein folding. Both alpha-helical and beta-sheet structures can be induced by the interaction of peptides or proteins with lipid surfaces. Melittin, the main component of bee venom, is a particularly well-studied example for the membrane-induced random coil-to-alpha-helix transition. Melittin in water adopts essentially a random coil conformation. The cationic amphipathic molecule has a high affinity for...
Paper Details
Title
Thermodynamics of melittin binding to lipid bilayers. Aggregation and pore formation.
Published Date
Mar 31, 2009
Volume
48
Issue
12
Pages
2586 - 2596
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