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Structural basis for the stability of a thermophilic methionine adenosyltransferase against guanidinium chloride
The methionine adenosyltransferase from the thermophile Methanococcus jannaschii is fully and irreversibly unfolded in the presence of guanidinium chloride. Unfolding of this dimeric protein is a three-state process in which a dimeric intermediate could be identified. The less stable secondary struc...
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| Main Authors: | , , , , |
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| Formato: | Artigo |
| Idioma: | Inglês |
| Publicado em: |
2010
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| Assuntos: | |
| Acesso em linha: | https://ncbi.nlm.nih.gov/pmc/articles/PMC3090699/ https://ncbi.nlm.nih.gov/pubmed/21132339 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1007/s00726-010-0813-y |
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