Intermediates in guanidine-HCl unfolding of glutamine synthetase from the extreme thermophile, Bacillus caldolyticus
Author:
Publisher
Elsevier BV
Subject
Molecular Biology,Biochemistry,Biophysics,Structural Biology
Reference22 articles.
1. Glutamine Synthetase of Escherichia Coli: Some Physical and Chemical Properties
2. The Enzymes of Glutamine Metabolism;Tate,1973
3. Two glutamine synthetases from Bacillus caldolyticus, an extreme thermophile. Isolation, physicochemical and kinetic properties.
4. Complementarity of regulation for the two glutamine synthetases from Bacillus caldolyticus, an extreme thermophile
Cited by 4 articles. 订阅此论文施引文献 订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献
1. Inactivation precedes conformation change during thermal denaturation of adenylate kinase;Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology;1993-06
2. Inactivation before significant conformational change during denaturation of papain by guanidine hydrochloride;Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology;1993-06
3. Control of enzyme activity in stirred bioreactors;The Chemical Engineering Journal;1993-02
4. Intermediates in denaturation of a small globular protein, recombinant human stefin B.;Journal of Biological Chemistry;1992-05
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