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Your search keyword '"Huang, Tsu-Wei"' showing total 13 results
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13 results on '"Huang, Tsu-Wei"'

8. Self-aligned wet-cell for hydrated microbiology observation in TEM

Author

Huang, Tsu-Wei, primary, Liu, Shih-Yi, additional, Chuang, Yun-Ju, additional, Hsieh, Hsin-Yi, additional, Tsai, Chun-Ying, additional, Huang, Yun-Tzu, additional, Mirsaidov, Utkur, additional, Matsudaira, Paul, additional, Tseng, Fan-Gang, additional, Chang, Chia-Shen, additional, and Chen, Fu-Rong, additional

Published
2012
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9. Fabrication and modification of dual-faced nano-mushrooms for tri-functional cell theranostics: SERS/fluorescence signaling, protein targeting, and drug delivery

Author

Hsieh, Hsin-Yi, primary, Huang, Tsu-Wei, additional, Xiao, Jian-Long, additional, Yang, Chung-Shi, additional, Chang, Chien-Cheng, additional, Chu, Chin-Chou, additional, Lo, Leu-Wei, additional, Wang, Shenq-Hann, additional, Wang, Pen-Cheng, additional, Chieng, Ching-Chang, additional, Lee, Chau-Hwang, additional, and Tseng, Fan-Gang, additional

Published
2012
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12. Distance Variations between Active Sites of H+-Pyrophosphatase Determined by Fluorescence Resonance Energy Transfer

Author

Huang, Yun-Tzu, primary, Liu, Tseng-Huang, additional, Chen, Yen-Wei, additional, Lee, Chien-Hsien, additional, Chen, Hsueh-Hua, additional, Huang, Tsu-Wei, additional, Hsu, Shen-Hsing, additional, Lin, Shih-Ming, additional, Pan, Yih-Jiuan, additional, Lee, Ching-Hung, additional, Hsu, Ian C., additional, Tseng, Fan-Gang, additional, Fu, Chien-Chung, additional, and Pan, Rong-Long, additional

Published
2010
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13. Distance Variations between Active Sites of H+-Pyrophosphatase Determined by Fluorescence Resonance Energy Transfer.

Author

Huang, Yun-Tzu, Liu, Tseng-Huang, Chen, Yen-Wei, Lee, Chien-Hsien, Chen, Hsueh-Hua, Huang, Tsu-Wei, Hsu, Shen-Hsing, Lin, Shih-Ming, Pan, Yih-Jiuan, Lee, Ching-Hung, Hsu, Lan C., Tseng, Fan-Gang, Fu, Chien-Chung, and Pan, Rong-Long

Subjects
*HOMEOSTASIS, *HYDROGEN-ion concentration, *ACIDITY function, *PYROPHOSPHATES, *POTASSIUM
Abstract

Homodimeric H+-pyrophosphatase (H+-PPase; EC 3.6.1.1) is a unique enzyme playing a pivotal physiological role in pH homeostasis of organisms. This novel H+-PPase supplies energy at the expense of hydrolyzing metabolic byproduct, pyrophosphate (PPi), for H+ translocation across membrane. The functional unit for the translocation is considered to be a homodimer. Its putative active site on each subunit consists of PPi binding motif, Acidic I and II motifs, and several essential residues. In this investigation structural mapping of these vital regions was primarily determined utilizing single molecule fluorescence resonance energy transfer. Distances between two C termini and also two N termini on homodimeric subunits of H+-ppase are 49.3 ± 4.0 and 67.2 ± 5.7 Å, respectively. Furthermore, putative PPi binding motifs on individual subunits are found to be relatively far away from each other (70.8 ± 4.8 Å), whereas binding of potassium and substrate analogue led them to closer proximity. Moreover, substrate analogue but not potassium elicits significant distance variations between two Acidic I motifs and two His-622 residues on homodimeric subunits. Taken together, this study provides the first quantitative measurements of distances between various essential motifs, residues, and putative active sites on homodimeric subunits of H+-PPase. A working model is accordingly proposed elucidating the distance variations of dimeric H+-PPase sup substrate binding. [ABSTRACT FROM AUTHOR]

Published
2010
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