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Affinity of IDPs to their targets is modulated by ion-specific changes in kinetics and residual structure
Intrinsically disordered proteins (IDPs) are characterized by a lack of defined structure. Instead, they populate ensembles of rapidly interconverting conformations with marginal structural stabilities. Changes in solution conditions such as temperature and crowding agents consequently affect IDPs m...
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| I publikationen: | Proc Natl Acad Sci U S A |
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| Huvudupphovsmän: | , , |
| Materialtyp: | Artigo |
| Språk: | Inglês |
| Publicerad: |
National Academy of Sciences
2017
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| Ämnen: | |
| Länkar: | https://ncbi.nlm.nih.gov/pmc/articles/PMC5604010/ https://ncbi.nlm.nih.gov/pubmed/28847960 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1073/pnas.1705105114 |
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