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Residual structure accelerates binding of intrinsically disordered ACTR by promoting efficient folding upon encounter
Intrinsically disordered proteins (IDPs) often fold into stable structures upon specific binding. The roles of residual structure of unbound IDPs in coupling binding and folding have been under much debate. While many studies emphasize the importance of conformational flexibility for IDP recognition...
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| Udgivet i: | J Mol Biol |
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| Main Authors: | , , |
| Format: | Artigo |
| Sprog: | Inglês |
| Udgivet: |
2018
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| Fag: | |
| Online adgang: | https://ncbi.nlm.nih.gov/pmc/articles/PMC6687458/ https://ncbi.nlm.nih.gov/pubmed/30528464 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1016/j.jmb.2018.12.001 |
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