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Drug Resistance Mutation L76V Decreases the Dimer Stability and Rate of Autoprocessing of HIV-1 Protease by Reducing Internal Hydrophobic Contacts
The mature HIV-1 protease (PR) bearing drug-resistance mutation L76V (PR(L76V)) is significantly less stable, with >7-fold higher dimer dissociation constant (K(d)) of 71 ± 24 nM and twice the sensitivity to urea denaturation (UC(50) = 0.85 M) relative to PR. Differential scanning calorimetry sho...
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| Autori principali: | , , , , , |
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| Natura: | Artigo |
| Lingua: | Inglês |
| Pubblicazione: |
2011
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| Soggetti: | |
| Accesso online: | https://ncbi.nlm.nih.gov/pmc/articles/PMC3101314/ https://ncbi.nlm.nih.gov/pubmed/21446746 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1021/bi200033z |
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