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Figure 5: General principles of protein adsorption on surface. The α-helices and β-sheets are stabilized by hydrogen bonds alone and these bonds combined with hydrophobic interaction. The protein tertiary structure (the hydrophobic core) is formed by hydrophobic interaction and further stabilized by disulfide linkages. The tertiary conformation is stabilized by hydrogen bonds and electrostatic interaction between side-chain amino acid residues and reinforced by Van der Waals interaction. So, the charged surface and hydrophobic surface have major effects on protein adsorption and conformation.