Protein stability remains one of the main factors limiting the realization of the full potential of protein therapeutics. Poly(ethylene glycol) (PEG) conjugation to proteins has evolved into an important tool to overcome instability issues associated with proteins. The observed increase in thermodyn
Solid-State Stabilization of α-Chymotrypsin and Catalase with Carbohydrates
✍ Scribed by Lee, Sau Lawrence; Hafeman, Andrea E.; Debenedetti, Pablo G.; Pethica, Brian A.; Moore, David J.
- Book ID
- 111869110
- Publisher
- American Chemical Society
- Year
- 2006
- Tongue
- English
- Weight
- 324 KB
- Volume
- 45
- Category
- Article
- ISSN
- 0888-5885
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a-Chymotrypsin has been modified with poly(ethylene glycols) and proxanols, block-copolymers of poly(propylene oxide) and poly(ethylene oxide). These conjugates were several-fold more thermostable and showed high catalytic activity at elevated concentrations of water-miscible organic cosolvents (alc
## Abstract **Summary:** The structure and stability of hydrogen bonds in __α__‐chitin were investigated by ^13^C solid‐state NMR measurements at different temperatures. Splitting of the carbonyl carbon signal for __α__‐chitin was interpreted as two types of hydrogen bonding; the peaks at 173.5 and