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Kinetically trapped metastable intermediate of a disulfide-deficient mutant of the starch-binding domain of glucoamylase
Refolding of a thermally unfolded disulfide-deficient mutant of the starch-binding domain of glucoamylase was investigated using differential scanning calorimetry, isothermal titration calorimetry, CD, and (1)H NMR. When the protein solution was rapidly cooled from a higher temperature, a kinetic in...
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| Main Authors: | , , , , , |
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| Formato: | Artigo |
| Idioma: | Inglês |
| Publicado em: |
Wiley Subscription Services, Inc., A Wiley Company
2009
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| Assuntos: | |
| Acesso em linha: | https://ncbi.nlm.nih.gov/pmc/articles/PMC2776959/ https://ncbi.nlm.nih.gov/pubmed/19530230 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1002/pro.188 |
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