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α-Crystallin binds to the aggregation-prone molten-globule state of alkaline protease: Implications for preventing irreversible thermal denaturation
α-Crystallin, the major eye-lens protein with sequence homology with heat-shock proteins (HSPs), acts like a molecular chaperone by suppressing the aggregation of damaged crystallins and proteins. To gain more insight into its chaperoning ability, we used a protease as the model system that is known...
Αποθηκεύτηκε σε:
| Κύριοι συγγραφείς: | , , |
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| Μορφή: | Artigo |
| Γλώσσα: | Inglês |
| Έκδοση: |
Cold Spring Harbor Laboratory Press
2002
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| Θέματα: | |
| Διαθέσιμο Online: | https://ncbi.nlm.nih.gov/pmc/articles/PMC2384148/ https://ncbi.nlm.nih.gov/pubmed/12070325 |
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