Aha1 Exhibits Distinctive Dynamics Behavior and Chaperone-Like Activity
نویسندگان
چکیده
منابع مشابه
Protein disulfide isomerase exhibits chaperone and anti-chaperone activity in the oxidative refolding of lysozyme.
Reduced, denatured lysozyme tends to aggregate at neutral pH, and competition between productive folding and aggregation substantially reduces the efficiency of refolding (Goldberg, M.E., Rudolph, R., and Jaenicke, R. (1991) Biochemistry 30, 2790-2797). Protein disulfide isomerase (PDI), a catalyst of oxidative protein folding, has a variety of effects on the yield of native lysozyme during the...
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ژورنال
عنوان ژورنال: Molecules
سال: 2021
ISSN: 1420-3049
DOI: 10.3390/molecules26071943