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 …