Two forms of the pH 4 folding intermediate of apomyoglobin
β Scribed by Marc Jamin; Robert L Baldwin
- Book ID
- 115628361
- Publisher
- Elsevier Science
- Year
- 1998
- Tongue
- English
- Weight
- 366 KB
- Volume
- 276
- Category
- Article
- ISSN
- 0022-2836
No coin nor oath required. For personal study only.
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## Abstract The molten globule model for the beginning of the folding process, which originated with Kuwajima's studies of __Ξ±__βlactalbumin (Kuwajima, K., 1989, __Proteins Struct. Funct. Genet. 6__, 87β103, and references therein), states that, for those proteins that exhibit equilibrium molten gl
## Abstract Temperatureβinduced denaturation transitions of different structural forms of apomyoglobin were studied monitoring intrinsic tryptophan fluorescence. It was found that the tryptophans are effectively screened from solvent both in native and acid forms throughout most of the temperature