## Abstract The adsorption of globular proteins at solid/liquid or liquid/liquid interfaces provides evidence of unfolded molecular conformation. Proteins with high apolar character are strongly unfolded, while those with high polar character are generally incompletely unfolded. Structural changes
Adsorption of crotonaldehyde at the mercury/water interface
โ Scribed by D. Gonzalez-Arjona; M. Rueda; R. Andreu
- Publisher
- Elsevier Science
- Year
- 1986
- Weight
- 945 KB
- Volume
- 199
- Category
- Article
- ISSN
- 0022-0728
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## Abstract The effect of cytochrome __c__ on the redox behavior of 1,4โbenzoquinone and cystine has been investigated by differential pulse polarography. The adsorption of cytochrome __c__ on mercury surface produces a lowering of the reduction peak of 1,4โbenzoquinone and of the cystine prepeak.
## dynamics are usually considerably changed by coadsorption The adsorption of a purified solution of octanoic acid at the (6,7). As already reported in (7) it is indispensable to use mercury/solution and air/water interfaces was studied. The equisurfactant solutions with a sufficient grade of pur