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Salvaging the Thermodynamic Destabilization of Interface Histidine in Transmembrane β-Barrels
[Image: see text] The ability of histidine to participate in a wide range of stabilizing polar interactions preferentially populates this residue in functionally important sites of proteins. Histidine possesses an amphiphilic and electrostatic nature that is essential for amino acids residing at mem...
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| Publicado no: | Biochemistry |
|---|---|
| Main Authors: | , , , , |
| Formato: | Artigo |
| Idioma: | Inglês |
| Publicado em: |
American
Chemical Society
2018
|
| Acesso em linha: | https://ncbi.nlm.nih.gov/pmc/articles/PMC6284319/ https://ncbi.nlm.nih.gov/pubmed/30284812 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1021/acs.biochem.8b00805 |
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