Abstract
We report the results of x-ray reflectivity measurements of thin films formed by different water-soluble proteins at the air–aqueous solution interface. It is demonstrated that glucose oxidase, alcohol dehydrogenase, and urease molecules denaturate at the air–aqueous solution interface to form 8- to 14-Å-thick peptide sheets. X-ray reflectivity data indicate that the spreading of a lipid monolayer at the aqueous solution surface before protein injection does not prevent proteins from unfolding. On the other hand, crosslinking of proteins results in intact enzyme layers at the subphase surface. A model that involves interaction of glucose oxidase molecules with a phospholipid monolayer is proposed. In this model, an observed decrease of the lipid electron density in the protein presence is explained in terms of “holes” in the monolayer film caused by protein molecule adsorption.
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Dates
Type | When |
---|---|
Created | 23 years ago (July 26, 2002, 10:39 a.m.) |
Deposited | 3 years, 4 months ago (April 13, 2022, 5:55 p.m.) |
Indexed | 3 weeks, 2 days ago (Aug. 2, 2025, 1:12 a.m.) |
Issued | 26 years, 5 months ago (March 16, 1999) |
Published | 26 years, 5 months ago (March 16, 1999) |
Published Online | 26 years, 5 months ago (March 16, 1999) |
Published Print | 26 years, 5 months ago (March 16, 1999) |
@article{Gidalevitz_1999, title={Protein folding at the air–water interface studied with x-ray reflectivity}, volume={96}, ISSN={1091-6490}, url={http://dx.doi.org/10.1073/pnas.96.6.2608}, DOI={10.1073/pnas.96.6.2608}, number={6}, journal={Proceedings of the National Academy of Sciences}, publisher={Proceedings of the National Academy of Sciences}, author={Gidalevitz, David and Huang, Zhengqing and Rice, Stuart A.}, year={1999}, month=mar, pages={2608–2611} }