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Thermal unfolding of dodecameric glutamine synthetase: inhibition of aggregation by urea.

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 a large irreversible transiti...

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Detalhes bibliográficos
Main Authors: Nosworthy, N. J., Ginsburg, A.
Formato: Artigo
Idioma:Inglês
Publicado em: Cold Spring Harbor Laboratory Press 1997
Assuntos:
Acesso em linha:https://ncbi.nlm.nih.gov/pmc/articles/PMC2143615/
https://ncbi.nlm.nih.gov/pubmed/9416610
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