Browsing by Author "Lin, Shih-Ming"

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Dual-focal-plane augmented reality head-up display using a single picture generation unit and a single freeform mirror
(2019-07-10)
Qin, Zong
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Lin, Shih-Ming
;
Lu, Kuang-Tso
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Chen, Cheng-Huan
;
Huang, Yi-Pai
Two or more focal planes are required in augmented reality head-up displays (AR HUDs) to respectively present basic and interactive driving information to car drivers; whereas, solutions using two separated picture generation units (PGUs) with two sets of optics incur increased cost, reduced reliability, and expanded volume. To develop an AR HUD using a single PGU and a single curved mirror, we propose to set two logically separated regions on a single PGU and optically relay one of them to a new position to create two focal planes. A single freeform mirror acquired through careful optical and mechanical design optimization produces high image quality in an eyebox of 120 mm by 60 mm, simultaneously for a far image (9 m, 10 degrees by 3 degrees) and a near image (2.5 m, 6 degrees by 2 degrees). Finally, an AR HUD product with a compact volume of 8.5 L is fabricated to experimentally verify the design. (C) 2019 Optical Society of America
Functional Investigation of Transmembrane Helix 3 in H+-Translocating Pyrophosphatase
(2013-12-01)
Lee, Ching-Hung
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Chen, Yen-Wei
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Huang, Yun-Tzu
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Pan, Yih-Jiuan
;
Lee, Chien-Hsien
H+-translocating pyrophosphatase (H+-PPase, EC 3.6.1.1) plays an important role in acidifying vacuoles by transporting protons across membranes at the expense of pyrophosphate (PPi) hydrolysis. Vigna radiata H+-PPase (VrH(+)-PPase) contains 16 transmembrane helices (TMs). The hydrophobicity of TM3 is relatively lower than that of most other TMs, and the amino acids in this TM are highly conserved in plants. Furthermore, TM5 and -6, which are the core TMs involving in H+-PPase functions, are near TM3. It is thus proposed that TM3 is associated with H+-PPase activity. To address this possibility, site-directed mutagenesis was applied in this investigation to determine the role of TM3 in VrH(+)-PPase. Upon alanine/serine substitution, T138 and S142, whose side chains face toward the center TMs, were found to be involved in efficient proton transport. G149/S153 and G160/A164 pairs at the crucial termini of the two GxxxG-like motifs are indispensable in maintaining enzymatic activities and conformational stability. Moreover, stability in the vicinity surrounding G149 is pivotal for efficient expression. S153, M161 and A164 are critical for the K+-mediated stimulation of H+-PPase. Taken together, our results demonstrate that TM3 plays essential roles in PPi hydrolysis, proton transport, expression, and K+ stimulation of H+-PPase.
The proximity between C-termini of dimeric vacuolar H(+)-pyrophosphatase determined using atomic force microscopy and a gold nanoparticle technique
(2009-08-01)
Liu, Tseng-Huang
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Hsu, Shen-Hsing
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Huang, Yun-Tzu
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Lin, Shih-Ming
;
Huang, Tsu-Wei
Vacuolar H(+)-translocating inorganic pyrophosphatase [vacuolar H(+)-pyrophosphatase (V-PPase); EC 3.6.1.1] is a homodimeric proton translocase; it plays a pivotal role in electrogenic translocation of protons from the cytosol to the vacuolar lumen, at the expense of PP(i) hydrolysis, for the storage of ions, sugars, and other metabolites. Dimerization of V-PPase is necessary for full proton translocation function, although the structural details of V-PPase within the vacuolar membrane remain uncertain. The C-terminus presumably plays a crucial role in sustaining enzymatic and proton-translocating reactions. We used atomic force microscopy to visualize V-PPases embedded in an artificial lipid bilayer under physiological conditions. V-PPases were randomly distributed in reconstituted lipid bilayers; approximately 43.3% of the V-PPase protrusions faced the cytosol, and 56.7% faced the vacuolar lumen. The mean height and width of the cytosolic V-PPase protrusions were 2.8 +/- 0.3 nm and 26.3 +/- 4.7 nm, whereas those of the luminal protrusions were 1.2 +/- 0.1 nm and 21.7 +/- 3.6 nm, respectively. Moreover, both C-termini of dimeric subunits of V-PPase are on the same side of the membrane, and they are close to each other, as visualized with antibody and gold nanoparticles against 6xHis tags on C-terminal ends of the enzyme. The distance between the V-PPase C-terminal ends was determined to be approximately 2.2 +/- 1.4 nm. Thus, our study is the first to provide structural details of a membrane-bound V-PPase dimer, revealing its adjacent C-termini.
The proximity between C-termini of dimeric vacuolar H+-pyrophosphatase determined using atomic force microscopy and a gold nanoparticle technique
(2009-08-01)
Liu, Tseng-Huang
;
Hsu, Shen-Hsing
;
Huang, Yun-Tzu
;
Lin, Shih-Ming
;
Huang, Tsu-Wei
Vacuolar H+-translocating inorganic pyrophosphatase [vacuolar H+-pyrophosphatase (V-PPase); EC 3.6.1.1] is a homodimeric proton translocase; it plays a pivotal role in electrogenic translocation of protons from the cytosol to the vacuolar lumen, at the expense of PPi hydrolysis, for the storage of ions, sugars, and other metabolites. Dimerization of V-PPase is necessary for full proton translocation function, although the structural details of V-PPase within the vacuolar membrane remain uncertain. The C-terminus presumably plays a crucial role in sustaining enzymatic and proton-translocating reactions. We used atomic force microscopy to visualize V-PPases embedded in an artificial lipid bilayer under physiological conditions. V-PPases were randomly distributed in reconstituted lipid bilayers; approximately 43.3% of the V-PPase protrusions faced the cytosol, and 56.7% faced the vacuolar lumen. The mean height and width of the cytosolic V-PPase protrusions were 2.8 +/- 0.3 nm and 26.3 +/- 4.7 nm, whereas those of the luminal protrusions were 1.2 +/- 0.1 nm and 21.7 +/- 3.6 nm, respectively. Moreover, both C-termini of dimeric subunits of V-PPase are on the same side of the membrane, and they are close to each other, as visualized with antibody and gold nanoparticles against 6xHis tags on C-terminal ends of the enzyme. The distance between the V-PPase C-terminal ends was determined to be approximately 2.2 +/- 1.4 nm. Thus, our study is the first to provide structural details of a membrane-bound V-PPase dimer, revealing its adjacent C-termini.
Tunable endothermic plateau for enhancing thermal energy storage obtained using binary metal alloy particles
(2016-07)
Lai, Chih-Chung
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Lin, Shih-Ming
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Chu, Yuan-Da
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Chang, Chun-Che
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Chueh, Yu-Lun
Thermal energy storage is crucial for various industrial systems. Enhancements in energy storage induced by latent heat have been demonstrated by using phase-change materials. However, these enhancements occur only at the melting points of the materials. In this study, we demonstrated the controllability of latent heat absorption/release in a certain temperature range. A wide endothermic plateau from 370 to 407 degrees C for the Hitec salt was obtained by releasing the latent heat of alloy particles embedded in the salt. The alloy particle-doped salt was applied to a Stirling engine to demonstrate its effectiveness in enhancing the energy and power outputs of the engine. Compared to pure salt, the alloy particle-doped salt can enhance the engine\'s energy output by 21%. With the advantages of scalable synthesis and superior thermal properties, the alloy particles have potential applications in energy storage enhancement in various thermal energy systems. (C) 2016 Published by Elsevier Ltd.