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Induction of changes in the secondary structure of globular proteins by a hydrophobic surface

โœ Scribed by Hua Wu; Yong Fan; Jun Sheng; Sen-Fang Sui

Publisher
Springer
Year
1993
Tongue
English
Weight
509 KB
Volume
22
Category
Article
ISSN
1432-1017

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โœฆ Synopsis

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 (~ helix and/~ 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 /~ structure, indicating that for certain proteins, the/3 structure may be a more stable secondary structure than ct helix on the hydrophobic surface.

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