Volume fraction of the polypeptide chain in proteins and the concentration of protein denaturants
β Scribed by D. E. Goldsack
- Publisher
- Wiley (John Wiley & Sons)
- Year
- 1968
- Tongue
- English
- Weight
- 122 KB
- Volume
- 6
- Category
- Article
- ISSN
- 0006-3525
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π SIMILAR VOLUMES
The topological aspects of the conformational transformations in a polypeptide chain are investigated in relation to the problem of selecting the minimum-energy pathways in protein folding.
The aim of this work was to provide a short overview of existing methods for the determination of free drug concentration and protein-drug binding fraction in plasma. Various methods have been described in terms of principles, evaluation of methods, and applications in recent years, with an emphasis
On page 717, line 3 in the figure caption of Figure 3 should read: PGA solution; On page 719, line 5 should read "the sites" rather thaii "three sites."
It is proposed that the thermally driven motion of certain polypeptide chains, including those that are part of an otherwise stable folded protein, produces timeaveraged three-dimensional domains that confer unique functions to a protein. These domains may be controlled by collapsing the polypeptide