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The charged amino acid residues such as tryptophan, aspartic acid, and glutamic acid in DSIP molecules may undergo changes in their charge distribution under the action of electromagnetic fields, thereby affecting the secondary structure (such as alpha helix and beta fold) and tertiary structure (spatial conformation determined by amino acid sequences, involving hydrophobic interactions, van der Waals forces, salt bridges, and other non covalent interactions) of DSIP

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