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Conformational stability changes of the amino terminal domain of enzyme I of the Escherichia coli phosphoenolpyruvate: sugar phosphotransferase system produced by substituting alanine or glutamate for the active-site histidine 189: implications for phosphorylation effects.
Ginsburg A, Szczepanowski RH, Ruvinov SB, Nosworthy NJ, Sondej M, Umland TC, Peterkofsky A. Ginsburg A, et al. Protein Sci. 2000 Jun;9(6):1085-94. doi: 10.1110/ps.9.6.1085. Protein Sci. 2000. PMID: 10892802 Free PMC article.
Thermal unfolding of dodecameric glutamine synthetase: inhibition of aggregation by urea.
Nosworthy NJ, Ginsburg A. Nosworthy NJ, et al. Among authors: ginsburg a. Protein Sci. 1997 Dec;6(12):2617-23. doi: 10.1002/pro.5560061213. Protein Sci. 1997. PMID: 9416610 Free PMC article.
Thermal unfolding of dodecameric manganese glutamine synthetase (622,000 M(r)) at pH 7 and approximately 0.02 ionic strength occurs in two observable steps: a small reversible transition (Tm approximately 42 degrees C; delta H approximately equal to 0.9 J/g) followed by …
Thermal unfolding of dodecameric manganese glutamine synthetase (622,000 M(r)) at pH 7 and approximately 0.02 ionic strength occurs in two o …
315 results