THE QUARTERNARY STRUCTURE OF TRYPTOPHAN SYNTHASE FROM ESCHERICHIA-COLI - FLUORESCENCE AND HYDRODYNAMIC STUDIES
- 1 January 1983
- journal article
- research article
- Vol. 129 (3) , 675-684
Abstract
No abstract availableThis publication has 25 references indexed in Scilit:
- Reversible unfolding of the β2 subunit of Escherichia coli tryptophan synthetase and its proteolytic fragmentsJournal of Molecular Biology, 1980
- Location of three active site residues in the NH2-terminal sequence of the beta 2 subunit tryptophan synthase from Escherichia coli.Journal of Biological Chemistry, 1980
- An active proteolytic derivative of the .alpha. subunit of tryptophan synthase. Identification of the site of cleavage and characterization of the fragmentsBiochemistry, 1979
- Conformational and ligand binding properties of the isolated domains from the beta 2 subunit of Escherichia coli tryptophan synthetase investigated by the reactivity of their cysteines.Journal of Biological Chemistry, 1979
- The orientational freedom of molecular probes. The orientation factor in intramolecular energy transferBiophysical Journal, 1979
- Affinity Chromatography of Tryptophan Synthase fromEscherichia coliEuropean Journal of Biochemistry, 1979
- Effect of the orientation of donor and acceptor on the probability of energy transfer involving electronic transitions of mixed polarizationBiochemistry, 1978
- Isolation and characterization of independently folding regions of the β chain of Escherichia coli tryptophan synthetaseBiochemistry, 1977
- A new thiol-dependent transamination reaction catalyzed by the B protein of Escherichia coli tryptophan synthetaseBiochemistry, 1968
- Frictional coefficients of multisubunit structures. I. TheoryBiopolymers, 1967