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- W2063493928 abstract "Abstract In this work we examine the binding and folding of the membrane-active peptide, melittin in the presence of ganglioside GM1 micelle. The membrane bilayer is capable of inducing folding to small proteins and peptides upon binding. Using two-dimensional NMR techniques we have shown that at low concentration, GM1 micelle is able to induce an extended helical conformation to MLT. The pulsed-field gradient diffusion NMR study indicates that the peptide partition into GM1 micelle along with about 32% binding. While looking for the binding between MLT and GM1 using saturation transfer difference NMR spectroscopy, Val5, Leu9, Thr11, Ile17, Ser18, and Trp19 have been identified as the residues that are in close proximity to GM1 micelles." @default.
- W2063493928 created "2016-06-24" @default.
- W2063493928 creator A5003506028 @default.
- W2063493928 creator A5082471813 @default.
- W2063493928 date "2005-10-01" @default.
- W2063493928 modified "2023-09-24" @default.
- W2063493928 title "Binding and Folding of Melittin in the Presence of Ganglioside GM1 Micelles" @default.
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- W2063493928 doi "https://doi.org/10.1080/07391102.2005.10507058" @default.
- W2063493928 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/16060692" @default.
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