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- Title
In situ measurement of conformational changes in proteins at liquid interfaces by circular dichroism spectroscopy.
- Authors
Damodaran, Srinivasan
- Abstract
A new circular dichroism (CD) spectroscopy technique for studying conformational changes in proteins in situ at the air–water interface is described. By using this technique, conformations of four proteins, viz., β-casein, bovine serum albumin (BSA), lysozyme, and fibrinogen in the adsorbed state at the air–water interface have been studied. β-Casein, which is predominantly in a disordered state in solution, assumes a β-sheet conformation at the air–water interface. On the other hand, lysozyme and fibrinogen, which are α+β-type proteins in solution, become β-type proteins by completely transforming their α-helix structure into β-sheets. Bovine serum albumin, which is an α-type protein in solution, loses its α-helix and becomes a disordered protein at the air–water interface. The results indicated that during unfolding and film formation at the interface, structural changes in proteins, regardless of their initial native state, follow the course of increasing β-sheet and disordered structure and decreasing α-helix content. Although this seems to be the general trend, the exceptional case of BSA suggests, however, that this is not universal.
- Subjects
SPECTRUM analysis; CONFORMATIONAL analysis; MOLECULAR rotation of proteins; BLOOD proteins; FIBRINOGEN; DENATURATION of proteins
- Publication
Analytical & Bioanalytical Chemistry, 2003, Vol 376, Issue 2, p182
- ISSN
1618-2642
- Publication type
Article
- DOI
10.1007/s00216-003-1873-6