Abstract
Circular dichroism, ellipsometry and radiolabeling techniques were employed to study the induction of changes in the secondary structure of BSA, myoglobin and cytochrome C by a hydrophobic surface. The results showed that adsorbed protein molecules lose their ordered native structure in the initial stage of adsorption and the structure appears to be a random or disordered conformation. Protein molecules adsorbed in later stages adopt a more ordered secondary structure (α helix and β structure). The changes of secondary structure of globular proteins induced by a hydrophobic surface can be explained by the steric interaction between adsorbed proteins as well as by hydrophobic interactions during the adsorption process. In addition, there is obviously an intermediate stage in which the protein molecules are mainly in the β structure, indicating that for certain proteins, the β structure may be a more stable secondary structure than α helix on the hydrophobic surface.
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Correspondence to: S.-F. Sui
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Wu, H., Fan, Y., Sheng, J. et al. Induction of changes in the secondary structure of globular proteins by a hydrophobic surface. Eur Biophys J 22, 201–205 (1993). https://doi.org/10.1007/BF00185781
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DOI: https://doi.org/10.1007/BF00185781