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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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| Hlavní autoři: | , |
|---|---|
| Médium: | Artigo |
| Jazyk: | Inglês |
| Vydáno: |
Cold Spring Harbor Laboratory Press
1997
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| Témata: | |
| On-line přístup: | https://ncbi.nlm.nih.gov/pmc/articles/PMC2143615/ https://ncbi.nlm.nih.gov/pubmed/9416610 |
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