The absorption of globular proteins
β Scribed by Alan J. Bennett
- Publisher
- Wiley (John Wiley & Sons)
- Year
- 1973
- Tongue
- English
- Weight
- 286 KB
- Volume
- 12
- Category
- Article
- ISSN
- 0006-3525
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β¦ Synopsis
Abstract
A series of experiments is suggested to elucidate further the nature of the adsorption of globular proteins on polar solid surfaces. Two ratios of surface energies and the total protein volume are used to characterize the expected form of the adsorbed species. A simple model calculation illustrates the approach.
π SIMILAR VOLUMES
The interpretation of A C 3 O (the free energy change for the reaction, globular conformation + randomly coiled conformation, in the absence of denaturant), in terms of the free energies of transfer of various parts of the protein molecule from water to denaturant solution, is unsatisfactory because
The heats of binding of protons m b to three globular proteins, lysozyme, chymotrysinogen A, and oxidized cytochrome c, from pH 11-2 or lower a t 25Β°C were determined by flow microcalorimetry. In addition, the acid-base titrations of cbymotrypsinogen A and oxidized cytochrome c were investigated und
## 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
The atomic structures of proteins epitomize the ideas of complexity and irregularity in three-dimensional objects. For such objects, size and shape are difficult to quantify, and therefore the development of unbiased parameters for these properties could facilitate their description. Statistical ana