The reversible refolding of a lysozyme derivative containing an extra crosslink between Glu 35 and Trp 108 was observed at pH 3.7 in solutions of 4.5M LiBr and 4.6M 1-PrOH. The rate constants of unfolding and folding for crosslinked lysozyme were compared with those for intact lysozyme. In LiBr solu
β¦ LIBER β¦
Inhibitor Binding in the Transition State for Unfolding of Adenosine Deaminase
β Scribed by E. Adler; R. Wolfenden
- Publisher
- Elsevier Science
- Year
- 1994
- Tongue
- English
- Weight
- 435 KB
- Volume
- 22
- Category
- Article
- ISSN
- 0045-2068
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