Conformational changes induced by domain assembly within the beta2 subunit of Escherichia coli tryptophan synthase analysed with monoclonal antibodies
Author:
Publisher
Wiley
Subject
Biochemistry
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1111/j.1432-1033.1986.tb10079.x/fullpdf
Reference21 articles.
1. Isolation and characterization of independently folding regions of the β chain of Escherichia coli tryptophan synthetase
2. Kinetics of renaturation and self-assembly of intermediates on the pathway of folding of the β2-subunit of Escherichia coli tryptophan-synthetase
3. Kinetics and importance of the dimerization step in the folding pathway of the β2 subunit of Escherichia coli tryptophan synthase
4. Immunochemical study of the β chain ofEscherichia coli tryptophan synthetase and its proteolytic fragments
5. Measurements of the true affinity constant in solution of antigen-antibody complexes by enzyme-linked immunosorbent assay
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