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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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Detalhes bibliográficos
Publicado no:J Phys Chem B
Main Authors: Vugmeyster, Liliya, Ostrovsky, Dmitry, Hoatson, Gina L., Qiang, Wei, Falconer, Isaac B.
Formato: Artigo
Idioma:Inglês
Publicado em: 2017
Assuntos:
Acesso em linha: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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