The location of tryptophanyl groups in human and bovine carbonic anhydrases
Author:
Publisher
Elsevier BV
Subject
Biochemistry, Genetics and Molecular Biology (miscellaneous)
Reference41 articles.
1. Crystal Structure of Human Carbonic Anhydrase C
2. The Optical Rotatory Dispersion of Bovine and Human Carbonic Anhydrase in the Ultraviolet Region
3. Human Carbonic Anhydrase. Protein Conformation and Metal Ion Binding*
Cited by 15 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. Thermodynamic Analysis of Protein Folding and Stability Using a Tryptophan Modification Protocol;Analytical Chemistry;2014-06-23
2. Characterization of folding intermediates of human carbonic anhydrase II: probing substructure by chemical labeling of sulfhydryl groups introduced by site-directed mutagenesis;Biochemistry;1993-01-12
3. Fine tuning of the catalytic properties of carbonic anhydrase. Studies of a Thr200 His variant of human isoenzyme II;European Journal of Biochemistry;1990-06
4. Ultraviolet difference spectroscopy of bovine carbonic anhydrase substituted with various divalent metals;Journal of Inorganic Biochemistry;1984-02
5. Interaction of the unique competitive inhibitor imidazole with human carbonic anhydrase B;Biochemistry;1977-12-01
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