Effects of pH Values on the Kinetics of Liquid‐Phase Chemical‐Enhanced Oxidation of GaAs

1999 ◽  
Vol 146 (6) ◽  
pp. 2328-2332 ◽  
Author(s):  
Hwei‐Heng Wang ◽  
Jau‐Yi Wu ◽  
Yeong‐Her Wang ◽  
Mau‐Phon Houng
2002 ◽  
Vol 23 (5) ◽  
pp. 237-239 ◽  
Author(s):  
Jau-Yi Wu ◽  
Hwei-Heng Wang ◽  
Po-Wen Sze ◽  
Yeong-Her Wang ◽  
Mau-Phon Houng

2004 ◽  
Vol 43 (7A) ◽  
pp. 4087-4091 ◽  
Author(s):  
Kuan-Wei Lee ◽  
Yeong-Her Wang ◽  
Mau-Phon Houng

2004 ◽  
Vol 48 (9) ◽  
pp. 1683-1686 ◽  
Author(s):  
Chih-Cheng Wang ◽  
Hou-Kuei Huang ◽  
Yeong-Her Wang ◽  
Mau-Phon Houng ◽  
Chang-Luen Wu ◽  
...  

2000 ◽  
Vol 39 (Part 1, No. 7B) ◽  
pp. 4477-4480 ◽  
Author(s):  
Hwei-Heng Wang ◽  
Dei-Wei Chou ◽  
Jau-Yi Wu ◽  
Yeong-Her Wang ◽  
Mau-Phon Houng

2008 ◽  
Vol 52 (2) ◽  
pp. 289-293 ◽  
Author(s):  
Jian-Jiun Huang ◽  
Dei-Wei Chou ◽  
Po-Wen Sze ◽  
Yeong-Her Wang

1998 ◽  
Vol 37 (Part 2, No. 1A/B) ◽  
pp. L67-L70 ◽  
Author(s):  
Hwei-Heng Wang ◽  
Chien-Jung Huang ◽  
Yeong-Her Wang ◽  
Mau-Phon Houng

2019 ◽  
Author(s):  
Joris van Lindt ◽  
Anna Bratek-Skicki ◽  
Donya Pakravan ◽  
Ludo Van Den Bosch ◽  
Dominique Maes ◽  
...  

Understanding the kinetics and underlying physicochemical forces of liquid-liquid phase separation (LLPS) is of paramount importance in cell biology, requiring reproducible methods for the analysis of often severely aggregation-prone proteins. Frequently applied approaches, such as dilution of the protein from an urea-containing solution or cleavage of its fused solubility tag, however, often lead to very different kinetic behaviors. Here we suggest that at extreme pH values even proteins such as the low-complexity domain (LCD) of hnRNPA2, TDP-43, and NUP-98 can be kept in solution, and then their LLPS can be induced by a jump to native pH, resulting in a system that can be easily controlled. This approach represents a generic method for studying LLPS under near native conditions, providing a platform for studying the phase-separation behavior of diverse proteins.


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