Pilosulin-4 incorporates both polar and hydrophobic elements that encourage helical formation in membrane models. Charge distribution promotes interaction profiling with lipid bilayers. Conformational patterns highlight structural motifs common to bioactive insect peptides. The fragment is applied in comparative venom research and peptide-engineering studies.
CAT No: P25009
1. TMEM16F and dynamins control expansive plasma membrane reservoirs
5. The spatiotemporal control of signalling and trafficking of the GLP-1R
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