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Pure Appl. Chem., 1995, Vol. 67, No. 11, pp. 1859-1866

http://dx.doi.org/10.1351/pac199567111859

Thermally induced unfolding of the tryptophan synthase α2β2 multienzyme complex from Salmonella typhimurium

D. P. Remeta, E. W. Miles and Ann Gisburg

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  • Quintyn Royston S., Zhou Mowei, Dagan Shai, Finke John, Wysocki Vicki H.: Ligand binding and unfolding of tryptophan synthase revealed by ion mobility-tandem mass spectrometry employing collision and surface induced dissociation. Int. J. Ion Mobil. Spec. 2013, 16, 133. <http://dx.doi.org/10.1007/s12127-013-0126-4>
  • Nishio Kazuya, Ogasahara Kyoko, Morimoto Yukio, Tsukihara Tomitake, Lee Soo Jae, Yutani Katsuhide: Large conformational changes in the Escherichia coli tryptophan synthase β2 subunit upon pyridoxal 5′-phosphate binding : Apo- and holo-tryptophan synthase β2 subunits. FEBS J 2010, 277, 2157. <http://dx.doi.org/10.1111/j.1742-4658.2010.07631.x>
  • Hioki Yusaku, Ogasahara Kyoko, Lee Soo Jae, Ma Jichun, Ishida Masami, Yamagata Yuriko, Matsuura Yoshiki, Ota Motonori, Ikeguchi Mitsunori, Kuramitsu Seiki: The crystal structure of the tryptophan synthase β2 subunit from the hyperthermophile Pyrococcus furiosus : Investigation of stabilization factors. Eur J Biochem 2004, 271, 2624. <http://dx.doi.org/10.1111/j.1432-1033.2004.04191.x>
  • Chen Chang-Hwei, Wu Susan J., Martin David L.: Structural Characteristics of Brain Glutamate Decarboxylase in Relation to Its Interaction and Activation. Archives of Biochemistry and Biophysics 1998, 349, 175. <http://dx.doi.org/10.1006/abbi.1997.0457>