Affinity purification and immobilization of fusion chaperonin GroEL-(His)6 and its utilization to mediate protein refolding
Author:
Publisher
Elsevier BV
Subject
Applied Microbiology and Biotechnology,Biotechnology
Reference23 articles.
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2. The crystal structure of the bacterial chaperonin GroEL at 2.8 A;Braig;Nature,1994
3. The crystal structure of the GroES co-chaperonin at 2.8 A resolution;Hunt;Nature,1996
4. Effects of the chaperonin GroE on the refolding of tryptophanase from Escherichia coli. Refolding is enhanced in the presence of ADP;Mizobata;J. Biol. Chem.,1992
5. The reaction cycle of GroEL and GroES in chaperonin-assisted protein folding;Martin;Nature,1993
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