Fluorescence and folding properties of Tyr mutant tryptophan synthase α-subunits from Escherichia coli
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry,Biophysics
Reference31 articles.
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4. Effects of the phenylalanine-22→leucine, glutamic acid-49→methionine, glycine-234→aspartic acid, and glycine-234→lysine mutations on the folding and stability of the α subunit of tryptophan synthase from Escherichia coli;Beasty;Biochemistry,1986
5. Equilibrium and kinetic analyses of unfolding and refolding for the conserved proline mutants of tryptophan synthase subunit;Ogasahara;Biochemistry,1997
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