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Dynamics of Hydrophobic Core Phenylalanine Residues Probed by Solid-State Deuteron NMR
We conducted a detailed investigation of the dynamics of two phenylalanine side chains in the hydrophobic core of the villin headpiece subdomain protein (HP36) in the hydrated powder state over the 298–80 K temperature range. Our main tools were static deuteron NMR measurements of longitudinal relax...
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| Publicado no: | J Phys Chem B |
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| Main Authors: | , , , , , , , |
| Formato: | Artigo |
| Idioma: | Inglês |
| Publicado em: |
2015
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| Assuntos: | |
| Acesso em linha: | https://ncbi.nlm.nih.gov/pmc/articles/PMC4970646/ https://ncbi.nlm.nih.gov/pubmed/26529128 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1021/acs.jpcb.5b09299 |
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