## 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
β¦ LIBER β¦
The core of apomyoglobin E-form folds at the diffusion limit
β Scribed by Gilmanshin, Rudolf; Callender, Robert H.; Dyer, R. Brian
- Book ID
- 109964842
- Publisher
- Nature Publishing Group
- Year
- 1998
- Tongue
- English
- Weight
- 287 KB
- Volume
- 5
- Category
- Article
- ISSN
- 1072-8368
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