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Allosteric stabilization of the amyloid-β peptide hairpin by the fluctuating N-terminal
Immobilized ions modulate nearby hydrophobic interactions and influence molecular recognition and self-assembly. We simulated disulfide bond-locked double mutants (L17C/L34C) and observed allosteric modulation of the peptide's intra-molecular interactions by the N-terminal tail. We revealed tha...
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| Publicado no: | Chem Commun (Camb) |
|---|---|
| Main Authors: | , , |
| Formato: | Artigo |
| Idioma: | Inglês |
| Publicado em: |
2015
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| Assuntos: | |
| Acesso em linha: | https://ncbi.nlm.nih.gov/pmc/articles/PMC4720562/ https://ncbi.nlm.nih.gov/pubmed/26666686 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1039/c5cc08107f |
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