Table 3: Secondary structure change through NM-protein interaction.

Secondary structure change NM-protein complex

-helix increases C60-HSA, SWNT-laccase.

-helix decreases Graphene-QDs-HSA, CdTe-QDs-HSA, Mercapto propionic acid-CdTe-QDs-HSA, Glutathione- CdTe-QDs-HSA, CDSe/ZnS-QDs-HSA, L-Cys capping CdTe-QDs-Lyz, CdS NP-HSA, CdS NP-BSA, N-Acetyl-L-cysteine-capped CdTe–BSA, N-Acetyl-L-cysteine-capped CdTe–BHb, N-Acetyl-L-cysteine-capped CdTe–catalase, CdTe–α-chymotrypsin, Cu–BSA, CuO–ß-galactosidase, ZnO–HSA, ZnO–lysozyme, ZnO–α-lactalbumin, ZnO–ToxRp, Ag–PVT–HSA, Ag–BHb, Ag–urease, Histidine capped Au-NPs–BSA, Au-NPs–BSA, γ-Fe2O3–fbrinogen, NH2–Fe3O4–BSA, Fe3O4–BSA, Fe3O4–tubulin, OH–MWCNTs–transferring, OH–MWCNT–BSA, Carboxylated-MWCNT–BSA, Carboxylated-SWCNT–BSA, OH–MWCNTs–Hb, OH–SWCNTs–Hb, OH–MWCNTs–Mb, OH–SWCNTs–Mb, NH2–PAMAM–insulin, CHP–HSA, CHCP–HSA

ß-sheet increases SWCNT–tau protein, ND–Hb, SWNT-laccsae, HAp-protease.

No change C60-BSA, L-Cys capping CdTe-QDs-BSA, CuO–BSA, Fe2O3–Hb, SWNT–Lyz, Oxidized SWNT–Lyz, MWCNT–tau protein, COOH–PAMAM–insulin, OH–PAMAM–insulin.