Pressure Induced Disorder in Kaolinite

Clay Minerals ◽  
1993 ◽  
Vol 28 (2) ◽  
pp. 311-319 ◽  
Author(s):  
A. La Iglesia

AbstractChanges caused by pressures between 0 and 20 K bar on two samples of kaolinite have been studied. Increased pressure causes the samples to lose crystallinity, shown by a decrease in the Hinckley, Lietard and reference intensity ratio indices, as well as by the crystallite size measured from the 001 reflection. Results from DTA and solid state NMR show slight or no differences between the compressed and natural samples. Nonetheless, thermogravimetry reveals that the pressure treatment lowers the temperature at which dehydroxylation begins, but, unlike the grinding process, pressure does not alter the OH content of the samples. As a result of the increase in pressure, the IR spectra of the samples show a gradual increase in the intensity of the band at 1104 cm -1 with respect to 1112 cm -1. An increase in intensity can also be observed in the band at 936 cm ~ with respect to the band at 912 cm -1. Examination by electron microscopy reveals the existence of a large number of defects such as fractures, bends and deformations of the sheets, etc.; these are responsible for the decrease in crystallinity.

2007 ◽  
Vol 1768 (12) ◽  
pp. 3012-3019 ◽  
Author(s):  
Sarika Shastri ◽  
Janet Vonck ◽  
Nicole Pfleger ◽  
Winfried Haase ◽  
Werner Kuehlbrandt ◽  
...  

Life ◽  
2021 ◽  
Vol 11 (9) ◽  
pp. 908
Author(s):  
Xing-Qi Dong ◽  
Jing-Yu Lin ◽  
Peng-Fei Wang ◽  
Yi Li ◽  
Jian Wang ◽  
...  

The succinate-acetate permease (SatP) is an anion channel with six transmembrane domains. It forms different oligomers, especially hexamers in the detergent as well as in the membrane. Solid-state NMR studies of SatP were carried out successfully on SatP complexes by reconstructing the protein into liposomes or retaining the protein in the native membrane of E. Coli., where it was expressed. The comparison of 13C-13C 2D correlation spectra between the two samples showed great similarity, opening the possibility to further study the acetate transport mechanism of SatP in its native membrane environment. Solid-state NMR studies also revealed small chemical shift differences of SatP in the two different membrane systems, indicating the importance of the lipid environment in determining the membrane protein structures and dynamics. Combining different 2D SSNMR spectra, chemical shift assignments were made on some sites, consistent with the helical structures in the transmembrane domains. In the end, we pointed out the limitation in the sensitivity for membrane proteins with such a size, and also indicated possible ways to overcome it.


1997 ◽  
Vol 30 (15) ◽  
pp. 4470-4480 ◽  
Author(s):  
Ioannis S. Polios ◽  
Maria Soliman ◽  
Chin Lee ◽  
Samuel P. Gido ◽  
Klaus Schmidt-Rohr ◽  
...  

1999 ◽  
Vol 1 (17) ◽  
pp. 3871-3878 ◽  
Author(s):  
Alexander DuChesne ◽  
Albena Bojkova ◽  
Jörg Rottstegge ◽  
Gunnar Glasser ◽  
Dieter Neher ◽  
...  

2017 ◽  
Vol 23 (14) ◽  
pp. 3280-3284 ◽  
Author(s):  
Brijith Thomas ◽  
Jeroen Rombouts ◽  
Gert T. Oostergetel ◽  
Karthick B. S. S. Gupta ◽  
Francesco Buda ◽  
...  

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