Dynamic mechanism of halide salts on the phase transition of protein models, poly(N-isopropylacrylamide) and poly(N,N-diethylacrylamide).
Journal
Physical chemistry chemical physics : PCCP
ISSN: 1463-9084
Titre abrégé: Phys Chem Chem Phys
Pays: England
ID NLM: 100888160
Informations de publication
Date de publication:
14 Jun 2020
14 Jun 2020
Historique:
pubmed:
28
5
2020
medline:
24
11
2020
entrez:
28
5
2020
Statut:
ppublish
Résumé
The effects of salts on protein systems are not yet fully understood. We investigated the ionic dynamics of three halide salts (NaI, NaBr, and NaCl) with two protein models, namely poly(N-isopropylacrylamide) (PNIPAM) and poly(N,N-diethylacrylamide) (PDEA), using multinuclear NMR, dispersion corrected density functional theory (DFT-D) calculations and dynamic light scattering (DLS) methods. The variation in ionic line-widths and chemical shifts induced by the polymers clearly illustrates that anions rather than cations interact directly with the polymers. From the variable temperature measurements of the NMR transverse relaxation rates of anions, which characterize the polymer-anion interaction intensities, the evolution behaviors of Cl
Substances chimiques
Acrylamides
0
Acrylic Resins
0
Bromides
0
Polymers
0
Proteins
0
Sodium Compounds
0
poly(N,N-diethylacrylamide)
0
poly-N-isopropylacrylamide
25189-55-3
Sodium Chloride
451W47IQ8X
Sodium Iodide
F5WR8N145C
sodium bromide
LC1V549NOM
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM