Comparison of Denaturation by Guanidine Hydrochloride of the Wild Type Tryptophan Synthase α-Subunit of Escherichia coli and Two Mutant Proteins (Glu 49—Met or Gln)
Author:
Publisher
Oxford University Press (OUP)
Subject
Molecular Biology,Biochemistry,General Medicine
Link
http://academic.oup.com/jb/article-pdf/85/4/915/2451257/85-4-915.pdf
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1. Strategy for cold adaptation of the tryptophan synthase α subunit from the psychrophile Shewanella frigidimarina K14-2: crystal structure and physicochemical properties;The Journal of Biochemistry;2013-12-05
2. Thermal denaturation of tryptophan synthase α-subunit;International Journal of Peptide and Protein Research;2009-01-12
3. Calorimetric study of tryptophan synthase α-subunit and two mutant proteins;International Journal of Peptide and Protein Research;2009-01-12
4. THERMOLYSIN AND BACILLUS SUBTILIS NEUTRAL PROTEASE;International Journal of Peptide and Protein Research;2009-01-12
5. Structural Basis for Catalysis by Tryptophan Synthase;Advances in Enzymology - and Related Areas of Molecular Biology;2006-11-22
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