Universal Size Dependence of Integral Enthalpy and Entropy for Solid–Solid Phase Transitions of Nanocrystals

2017 ◽  
Vol 121 (44) ◽  
pp. 24831-24836 ◽  
Author(s):  
Zixiang Cui ◽  
Huijuan Duan ◽  
Qingshan Fu ◽  
Yongqiang Xue ◽  
Shuting Wang
1997 ◽  
Vol 52 (8-9) ◽  
pp. 679-680 ◽  
Author(s):  
Hiroyuki Ishida ◽  
Hiroshi Ono ◽  
Ryuichi Ikeda

Abstract The crystal structure of the highest-and second highest-temperature solid phases of choline tetrafluoroborate and iodide was determined by X-ray powder diffraction. The structure in the highest-temperature phase of both salts is NaCl-type cubic (a = 10.16(2) Å, Z = 4 for tetrafluorobo-rate; a = 10.08(2) Å, Z = 4 for iodide). The second highest-temperature phase of tetrafluoroborate and iodide is CsCl-type cubic (a = 6.198(6) Å and Z = 1) and tetragonal (a = 8.706(2) Å, c = 6.144(6) Å, and Z = 2), respectively. DSC was carried out for the iodide, where the presence of three solid-solid phase transitions was confirmed. Enthalpy and entropy changes of these transitions were evaluated.


Biomolecules ◽  
2021 ◽  
Vol 11 (7) ◽  
pp. 1014
Author(s):  
Macy L. Sprunger ◽  
Meredith E. Jackrel

Aberrant protein folding underpins many neurodegenerative diseases as well as certain myopathies and cancers. Protein misfolding can be driven by the presence of distinctive prion and prion-like regions within certain proteins. These prion and prion-like regions have also been found to drive liquid-liquid phase separation. Liquid-liquid phase separation is thought to be an important physiological process, but one that is prone to malfunction. Thus, aberrant liquid-to-solid phase transitions may drive protein aggregation and fibrillization, which could give rise to pathological inclusions. Here, we review prions and prion-like proteins, their roles in phase separation and disease, as well as potential therapeutic approaches to counter aberrant phase transitions.


2018 ◽  
Author(s):  
P. Bowlan ◽  
L. Smilowitz ◽  
B. F. Henson ◽  
N. Suvorova ◽  
D. Oschwald

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