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Analysis of βB1-crystallin unfolding equilibrium by spin and fluorescence labeling. Evidence of a dimeric intermediate.
A central step in understanding lens aging is to characterize the thermodynamic stability of its proteins and determine the consequences of changes in the primary sequence on their folding equilibria. For this purpose, destabilized mutations were introduced in βB1-crystallin targeting the domain int...
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| Hlavní autoři: | , , |
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| Médium: | Artigo |
| Jazyk: | Inglês |
| Vydáno: |
2007
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| Témata: | |
| On-line přístup: | https://ncbi.nlm.nih.gov/pmc/articles/PMC2394508/ https://ncbi.nlm.nih.gov/pubmed/17448466 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1016/j.febslet.2007.04.004 |
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