Denaturation of subtilisin BPN′ and its derivatives in aqueous guanidine hydrochloride solutions
✍ Scribed by Atsushi Ikai
- Book ID
- 115734225
- Publisher
- Elsevier Science
- Year
- 1976
- Weight
- 700 KB
- Volume
- 445
- Category
- Article
- ISSN
- 0005-2744
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higher temperatures. The data presented here might be used to understand better, through the application of different models, the exposure of non-polar amino acid side chains from the protein interior to the aqueous environment, which characterizes protein denaturation.
The spin-lattice relaxation times (TI) of the 170 nucleus of a water molecule in guanidine hydrochloride, urea, and alkylated ureas at 25 \*C were measured by NMR spectroscopy. Urea has no significant effect on the water structure. Also, guanidine hydrochloride as a stronger denaturant than urea doe