Study of interface effects in thermoelectric microrefrigerators

2000 ◽  
Vol 88 (7) ◽  
pp. 4135 ◽  
Author(s):  
Y. Sungtaek Ju ◽  
Uttam Ghoshal
Keyword(s):  
Interface Effects

Interface effects on the phase transition of MnS nanocrystal

2021 ◽  
Vol 23 ◽  
pp. 101015
Author(s):  
Ye Yuan ◽  
Xu Yan ◽  
Yongjing Wang ◽  
Yansong Xiong ◽  
Chen Tian ◽  
...  
Keyword(s):  
Phase Transition ◽  
Interface Effects

Debonding Behaviors of CFRP Strengthened RC Beams with Weak Interfaces

2013 ◽  
Vol 351-352 ◽  
pp. 587-591
Author(s):  
Sen Li ◽  
Xiao Gang Wang ◽  
Xin Gang Zhou
Keyword(s):  
Tensile Strain ◽  
Structural Integrity ◽  
Structural Performance ◽  
Rc Beams ◽  
Test Results ◽  
Weak Interface ◽  
Premature Rupture ◽  
Loading Process ◽  
Interface Effects

Debonding behaviors of CFRP strengthened RC beams were experimentally investigated under the influence of weak interfaces, which are induced either by defective bonding of replaced cover or expansive cracks. Shown by test results, weak interfaces impaired considerably the structural integrity of strengthening systems during loading, and easily led to CFRP debonding failure. U-strips worked effectively in preventing the integral debonding and guarantee the structural performance of flexural sheets. However, local cover delamination in the loading process and premature rupture of flexural CFRP could still take place due to the weak interface effects. Therefore, allowable tensile strain of flexural CFRP should be reduced, and more strict confinement and anchorage measures should be taken in this case.

Interface effects in the formation of silicon oxide on metal silicide layers over silicon substrates

1983 ◽  
Vol 54 (4) ◽  
pp. 1849-1854 ◽  
Author(s):  
J. E. E. Baglin ◽  
F. M. d’Heurle ◽  
C. S. Petersson
Keyword(s):  
Silicon Oxide ◽  
Silicon Substrates ◽  
Metal Silicide ◽  
Interface Effects

Reversed interface effects in amorphous FeZr/AlZr multilayers

2014 ◽  
Vol 90 (18) ◽  
Author(s):  
Martina Ahlberg ◽  
Atieh Zamani ◽  
Erik Östman ◽  
Hossein Fashandi ◽  
Björgvin Hjörvarsson ◽  
...  
Keyword(s):  
Interface Effects

scholarly journals Structures of designed armadillo-repeat proteins show propagation of inter-repeat interface effects

2016 ◽  
Vol 72 (1) ◽  
pp. 168-175 ◽  
Author(s):  
Christian Reichen ◽  
Chaithanya Madhurantakam ◽  
Simon Hansen ◽  
Markus G. Grütter ◽  
Andreas Plückthun ◽  
...  
Keyword(s):  
Second Generation ◽  
Body Movement ◽  
Recognition System ◽  
Third Generation ◽  
Peptide Recognition ◽  
Repeat Proteins ◽  
Peptide Binding Site ◽  
Armadillo Repeat ◽  
The Stability ◽  
Interface Effects

The armadillo repeat serves as a scaffold for the development of modular peptide-recognition modules. In order to develop such a system, three crystal structures of designed armadillo-repeat proteins with third-generation N-caps (YIII-type), four or five internal repeats (M-type) and second-generation C-caps (AII-type) were determined at 1.8 Å (His-YIIIM4AII), 2.0 Å (His-YIIIM5AII) and 1.95 Å (YIIIM5AII) resolution and compared with those of variants with third-generation C-caps. All constructs are full consensus designs in which the internal repeats have exactly the same sequence, and hence identical conformations of the internal repeats are expected. The N-cap and internal repeats M1to M3are indeed extremely similar, but the comparison reveals structural differences in internal repeats M4and M5and the C-cap. These differences are caused by long-range effects of the C-cap, contacting molecules in the crystal, and the intrinsic design of the repeat. Unfortunately, the rigid-body movement of the C-terminal part impairs the regular arrangement of internal repeats that forms the putative peptide-binding site. The second-generation C-cap improves the packing of buried residues and thereby the stability of the protein. These considerations are useful for future improvements of an armadillo-repeat-based peptide-recognition system.

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