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Dynamic profile analysis to characterize dynamics-driven allosteric sites in enzymes
We examine the dynamic features of non-trivial allosteric binding sites to elucidate potential drug binding sites. These allosteric sites were previously found to be allosteric after determination of the protein-drug co-crystal structure. After comprehensive search in the Protein Data Bank, we ident...
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| Опубликовано в: : | Biophys Physicobiol |
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| Главные авторы: | , |
| Формат: | Artigo |
| Язык: | Inglês |
| Опубликовано: |
The Biophysical Society of Japan (BSJ)
2016
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| Предметы: | |
| Online-ссылка: | https://ncbi.nlm.nih.gov/pmc/articles/PMC5042162/ https://ncbi.nlm.nih.gov/pubmed/27924265 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.2142/biophysico.13.0_117 |
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