scholarly journals Characterization of Thermal Transport in One-dimensional Solid Materials

10.3791/51144 ◽  
2014 ◽  
Author(s):  
Guoqing Liu ◽  
Huan Lin ◽  
Xiaoduan Tang ◽  
Kevin Bergler ◽  
Xinwei Wang
Keyword(s):  
Thermal Transport ◽  
Solid Materials ◽  
One Dimensional

Characterization of Minimum Route MTM in One-Dimensional Multi-Hop Wireless Networks

2009 ◽  
Vol E92-A (9) ◽  
pp. 2227-2235 ◽  
Author(s):  
Kazuyuki MIYAKITA ◽  
Keisuke NAKANO ◽  
Masakazu SENGOKU ◽  
Shoji SHINODA
Keyword(s):  
Wireless Networks ◽  
One Dimensional

Characterization of Thermal Transport in Carbon Nanotube Yarns

2014 ◽  
Author(s):  
Jianli Wang ◽  
Sisi He ◽  
Jiajian Bao ◽  
Xing Zhang ◽  
Juekuan Yang ◽  
...  
Keyword(s):  
Carbon Nanotube ◽  
Thermal Transport ◽  
Carbon Nanotube Yarns

Solvothermal Synthesis and Characterization of an One-Dimensional Zinc Phosphate

2002 ◽  
Vol 37 (2-3) ◽  
pp. 169-175 ◽  
Author(s):  
K. Yanxiong ◽  
L. Jianmin ◽  
Z. Yugen ◽  
H. Gaofei ◽  
J. Zheng ◽  
...  
Keyword(s):  
Solvothermal Synthesis ◽  
Zinc Phosphate ◽  
Synthesis And Characterization ◽  
One Dimensional

scholarly journals Synthesis and Structural Characterization of (E)-4-[(2-Hydroxy-3-methoxybenzylidene)amino]butanoic Acid and Its Novel Cu(II) Complex

Molbank ◽  
10.3390/m1179 ◽  
2021 ◽  
Vol 2021 (1) ◽  
pp. M1179
Author(s):  
Eleftherios Halevas ◽  
Antonios Hatzidimitriou ◽  
Barbara Mavroidi ◽  
Marina Sagnou ◽  
Maria Pelecanou ◽  
...  
Keyword(s):  
Schiff Base ◽  
Gamma Aminobutyric Acid ◽  
X Ray Diffraction ◽  
Reaction Conditions ◽  
Polymeric Compound ◽  
Bridging Ligands ◽  
1H And 13C Nmr ◽  
One Dimensional ◽  
Ft Ir

A novel Cu(II) complex based on the Schiff base obtained by the condensation of ortho-vanillin with gamma-aminobutyric acid was synthesized. The compounds are physico-chemically characterized by elemental analysis, HR-ESI-MS, FT-IR, and UV-Vis. The complex and the Schiff base ligand are further structurally identified by single crystal X-ray diffraction and 1H and 13C-NMR, respectively. The results suggest that the Schiff base are synthesized in excellent yield under mild reaction conditions in the presence of glacial acetic acid and the crystal structure of its Cu(II) complex reflects an one-dimensional polymeric compound. The molecular structure of the complex consists of a Cu(II) ion bound to two singly deprotonated Schiff base bridging ligands that form a CuN2O4 chelation environment, and a coordination sphere with a disordered octahedral geometry.

2D Self-assembly and Electronic Characterization of Oxygen-Boron-Oxygen-Doped Chiral Graphene Nanoribbons

2021 ◽  
Author(s):  
Lei Jin ◽  
Nerea Bilbao ◽  
Yang Lv ◽  
Xiao-Ye Wang ◽  
Soltani Paniz ◽  
...  
Keyword(s):  
Edge Effects ◽  
Self Assembly ◽  
Quantum Confinement ◽  
Graphene Nanoribbons ◽  
One Dimensional ◽  
The Past ◽  
Different Types

Graphene nanoribbons (GNRs), quasi-one-dimensional strips of graphene, exhibit a nonzero bandgap due to quantum confinement and edge effects. In the past decade, different types of GNRs with atomically precise structures...

scholarly journals Characterization of calcium-dependent membrane binding proteins of brain cortex

1985 ◽  
Vol 229 (3) ◽  
pp. 587-593 ◽  
Author(s):  
A R Rhoads ◽  
M Lulla ◽  
P B Moore ◽  
C E Jackson
Keyword(s):  
Brain Cortex ◽  
Peptide Mapping ◽  
Bovine Brain ◽  
Particulate Fraction ◽  
Structural Homology ◽  
One Dimensional ◽  
Calcium Dependent ◽  
Stokes Radius ◽  
The Brain

Proteins of Mr 68 000, 34 000 and 32 000 were selectively extracted by EGTA from brain cortex. The three proteins that were extracted along with calmodulin were acidic, monomeric, and did not exhibit structural homology, as demonstrated by one-dimensional peptide mapping. The Mr-68 000 protein was purified to homogeneity and had a Stokes radius of 3.54 nm and S20,W value of 5.1S. Purified calmodulin, Mr-68 000 protein and two proteins of Mr 34 000 and Mr 32 000, interacted with the brain particulate fraction, with half-maximal binding occurring at 3.5 microM, 8.3 microM and 150 microM-Ca2+ respectively. Proteins were bound independently of each other and calmodulin. Pretreatment of the particulate fraction with trypsin prevented the Ca2+-dependent binding of calmodulin; however, the binding of the Mr-68 000 protein or the Mr−32 000 and −34 000 proteins was unaffected. The Mr-68 000 protein of bovine brain did not cross-react immunologically with Mr-67 000 calcimedin from chicken gizzard.

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