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Solvent-Driven Dynamical Cross-Over in the Phenylalanine Side-Chain from the Hydrophobic Core of Amyloid Fibrils Detected by (2)H NMR Relaxation
Aromatic residues are important markers of dynamical changes in proteins’ hydrophobic cores. In this work we investigated the dynamics of the F19 side-chain in the core of amyloid fibrils across a wide temperature range of 300 to 140 K. We utilized solid-state (2)H NMR relaxation to demonstrate the...
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| Vydáno v: | J Phys Chem B |
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| Hlavní autoři: | , , , , |
| Médium: | Artigo |
| Jazyk: | Inglês |
| Vydáno: |
2017
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| Témata: | |
| On-line přístup: | https://ncbi.nlm.nih.gov/pmc/articles/PMC5567839/ https://ncbi.nlm.nih.gov/pubmed/28699757 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1021/acs.jpcb.7b04726 |
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