Oligomeric and Thermal Stability of TRPA1 Coiled-Coil Domain by Polyphosphates

GemC1, together with Idas and Geminin, an important regulator of DNA-replication licensing and differentiation decisions, constitute a superfamily sharing a homologous central coiled-coil domain. To better understand this family of proteins, the crystal structure of a GemC1 coiled-coil domain variant engineered for better solubility was determined to 2.2 Å resolution. GemC1 shows a less typical coiled coil compared with the Geminin homodimer and the Geminin–Idas heterodimer structures. It is also shown that both in vitro and in cells GemC1 interacts with Geminin through its coiled-coil domain, forming a heterodimer that is more stable that the GemC1 homodimer. Comparative analysis of the thermal stability of all of the possible superfamily complexes, using circular dichroism to follow the unfolding of the entire helix of the coiled coil, or intrinsic tryptophan fluorescence of a unique conserved N-terminal tryptophan, shows that the unfolding of the coiled coil is likely to take place from the C-terminus towards the N-terminus. It is also shown that homodimers show a single-state unfolding, while heterodimers show a two-state unfolding, suggesting that the dimer first falls apart and the helices then unfold according to the stability of each protein. The findings argue that Geminin-family members form homodimers and heterodimers between them, and this ability is likely to be important for modulating their function in cycling and differentiating cells.

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The Ordered Phase Formation in Ti-Al-Ga Alloys

Proceedings, annual meeting, Electron Microscopy Society of America ◽

10.1017/s0424820100069193 ◽

1970 ◽

Vol 28 ◽

pp. 440-441

Author(s):

Shiro Fujishiro ◽

Harold L. Gegel

Keyword(s):

Thermal Stability ◽

High Temperature ◽

Titanium Alloys ◽

Growth Kinetics ◽

Stoichiometric Composition ◽

Good Potential ◽

Alpha Titanium ◽

Cold Rolled ◽

Kinetics Of ◽

Thermal Stability Of

Ordered-alpha titanium alloys having a DO19 type structure have good potential for high temperature (600°C) applications, due to the thermal stability of the ordered phase and the inherent resistance to recrystallization of these alloys. Five different Ti-Al-Ga alloys consisting of equal atomic percents of aluminum and gallium solute additions up to the stoichiometric composition, Ti3(Al, Ga), were used to study the growth kinetics of the ordered phase and the nature of its interface.The alloys were homogenized in the beta region in a vacuum of about 5×10-7 torr, furnace cooled; reheated in air to 50°C below the alpha transus for hot working. The alloys were subsequently acid cleaned, annealed in vacuo, and cold rolled to about. 050 inch prior to additional homogenization

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Microstructure studies of tungsten silicide schottky contacts on Gaas

Proceedings, annual meeting, Electron Microscopy Society of America ◽

10.1017/s0424820100126445 ◽

1987 ◽

Vol 45 ◽

pp. 328-329

Author(s):

Yih-Cheng Shih ◽

E. L. Wilkie

Keyword(s):

Thermal Stability ◽

Field Effect Transistors ◽

Schottky Contact ◽

Schottky Contacts ◽

Excellent Thermal Stability ◽

Barrier Heights ◽

Gaas Substrates ◽

Film Adhesion ◽

Threshold Voltages ◽

Thermal Stability Of

Tungsten silicides (WSix) have been successfully used as the gate materials in self-aligned GaAs metal-semiconductor-field- effect transistors (MESFET). Thermal stability of the WSix/GaAs Schottky contact is of major concern since the n+ implanted source/drain regions must be annealed at high temperatures (∼ 800°C). WSi0.6 was considered the best composition to achieve good device performance due to its low stress and excellent thermal stability of the WSix/GaAs interface. The film adhesion and the uniformity in barrier heights and ideality factors of the WSi0.6 films have been improved by depositing a thin layer of pure W as the first layer on GaAs prior to WSi0.6 deposition. Recently WSi0.1 has been used successfully as the gate material in 1x10 μm GaAs FET's on the GaAs substrates which were sputter-cleaned prior to deposition. These GaAs FET's exhibited uniform threshold voltages across a 51 mm wafer with good film adhesion after annealing at 800°C for 10 min.

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TMCC3 localizes at the three-way junctions for the proper tubular network of the endoplasmic reticulum

Biochemical Journal ◽

10.1042/bcj20190359 ◽

2019 ◽

Vol 476 (21) ◽

pp. 3241-3260

Author(s):

Sindhu Wisesa ◽

Yasunori Yamamoto ◽

Toshiaki Sakisaka

Keyword(s):

Endoplasmic Reticulum ◽

Membrane Proteins ◽

Membrane Protein ◽

Mammalian Cells ◽

Coiled Coil ◽

Transmembrane Domains ◽

Domain Family ◽

Coiled Coil Domain ◽

U2os Cells ◽

Er Membrane

The tubular network of the endoplasmic reticulum (ER) is formed by connecting ER tubules through three-way junctions. Two classes of the conserved ER membrane proteins, atlastins and lunapark, have been shown to reside at the three-way junctions so far and be involved in the generation and stabilization of the three-way junctions. In this study, we report TMCC3 (transmembrane and coiled-coil domain family 3), a member of the TEX28 family, as another ER membrane protein that resides at the three-way junctions in mammalian cells. When the TEX28 family members were transfected into U2OS cells, TMCC3 specifically localized at the three-way junctions in the peripheral ER. TMCC3 bound to atlastins through the C-terminal transmembrane domains. A TMCC3 mutant lacking the N-terminal coiled-coil domain abolished localization to the three-way junctions, suggesting that TMCC3 localized independently of binding to atlastins. TMCC3 knockdown caused a decrease in the number of three-way junctions and expansion of ER sheets, leading to a reduction of the tubular ER network in U2OS cells. The TMCC3 knockdown phenotype was partially rescued by the overexpression of atlastin-2, suggesting that TMCC3 knockdown would decrease the activity of atlastins. These results indicate that TMCC3 localizes at the three-way junctions for the proper tubular ER network.

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