Low‐field NMR and FT‐IR Determination relationship between Water Migration and Protein Conformation of the preparation of minced meat

Author(s):  
Jinyue Zheng ◽  
Sun Di ◽  
Dengyong Liu ◽  
Jingxin Sun ◽  
Jun‐Hua Shao
2020 ◽  
Vol 2 (2) ◽  
pp. 17

Aqueous self-assembly customarily focuses on the molecular interactions of assembling building blocks; the role of water is barely studied. The hydration of hydrophobic P+X- (P+: macromolecular phosphonium cation, X-: anion) is dependent on the ionic end groups, which is responsible for the consequent assembling behavior. The water interaction with the backbone was analyzed by FT-IR, and the dynamics were measured by low field-NMR spectroscopy. The combination of these two techniques reveals the effect of X- on hydration. When X- is I-, the ionic end group ordered water molecules that exerted a detectable long-range effect de-hydrating the backbone. The consequent hydrophobic interaction drove the aqueous assembly of P+I- into micelle-like aggregates with the ionic group exposed to water. In contrast, the ion pair with a hydrophobic anion of [BPh4]- was not able to hold water and did not deplete the hydration water. The hydrated backbone of P+[BPh4]- assembled into vesicles that were driven by hydration interactions. This elucidation at the molecular level is craved to progress aqueous supramolecular chemistry.


2006 ◽  
Vol 183 (1) ◽  
pp. 134-141 ◽  
Author(s):  
P.L. Volegov ◽  
A.N. Matlachov ◽  
R.H. Kraus

2006 ◽  
Author(s):  
R. Guo ◽  
K. Mannhardt ◽  
A. Kantzas
Keyword(s):  

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