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Hydrophobic residues of melittin mediate its binding to αA−crystallin
The molecular chaperone αA‐crystallin, mainly localized in the human ocular lens, is believed to protect the lens from opacification and cataract, by suppressing the aggregation of the other lens proteins. The present study provides structural and thermodynamic insights into the ability of human αA‐...
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| Pubblicato in: | Protein Sci |
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| Autori principali: | , , |
| Natura: | Artigo |
| Lingua: | Inglês |
| Pubblicazione: |
John Wiley & Sons, Inc.
2019
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| Soggetti: | |
| Accesso online: | https://ncbi.nlm.nih.gov/pmc/articles/PMC6954717/ https://ncbi.nlm.nih.gov/pubmed/31762096 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1002/pro.3792 |
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