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RISS 인기검색어
- 검색키워드
- 저자 : Mandal Subhas Chandra (검색결과 3 건)
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Pabitra Kumar Mandal,Sayantan Sengupta,Subhas Chandra Rana,Dipankar Bhanja 대한기계학회 2021 JOURNAL OF MECHANICAL SCIENCE AND TECHNOLOGY Vol.35 No.11
The present problem is devoted to establish the effect of orientation on thermohydraulic performance of a horizontal heat sink with vertical pin-fin-array under forced convective environment. The fins are embedded on the base-plate of the heat sink in inline and staggered manner. When air passes over the fin-arrays it convects the heat conducted from the solid base-plate to the fins’ surface. Both the experimental and numerical studies have been performed under the same geometric configurations of the test plate and an acceptable agreement in results is obtained. To examine the influence of the orientation angle ( β ) on system performance, the heat sink is rotated anticlockwise in a regular interval from 0° to 360° about a vertical axis passing through the centre of the sink. The study has been performed over a large number of incoming Reynolds numbers (Re = 8500 to 38500) to investigate the possibility to achieve an optimal angle of orientation when Nusselt number (Nu) is maximum. Test results show that thermal dissipation attains maximum value at β = 40° for the inline array and that for β = 120° in case of staggered array. For low Reynolds number values (Re = 8500), the system performance is found better at an angle 35° and 120° for inline and staggered arrangement respectively. However, with Re = 38500, the maximum system performance is achieved at an angle 10° and 240° for inline and staggered arrangement respectively.
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Studies on Synonymous Codon and Amino Acid Usage Biases in the Broad-Host Range Bacteriophage KVP40
Sau Keya,Gupta Sanjib Kumar,Sau Subrata,Mandal Subhas Chandra,Ghosh Tapash Chandra The Microbiological Society of Korea 2007 The journal of microbiology Vol.45 No.1
In this study, the relative synonymous codon and amino acid usage biases of the broad-host range phage, KVP40, were investigated in an attempt to understand the structure and function of its proteins/protein-coding genes, as well as the role of its tRNAs. Synonymous codons in KVP40 were determined to be AT-rich at the third codon positions, and their variations are dictated principally by both mutational bias and translational selection. Further analysis revealed that the RSCU of KVP40 is distinct from that of its Vibrio hosts, V. cholerae and V. parahaemolyticus. Interestingly, the expression of the putative highly expressed genes of KVP40 appear to be preferentially influenced by the abundant host tRNA species, whereas the tRNAs expressed by KVP40 may be required for the efficient synthesis of all its proteins in a diverse array of hosts. The data generated in this study also revealed that KVP40 proteins are rich in low molecular weight amino acid residues, and that these variations are influenced primarily by hydropathy, mean molecular weight, aromaticity, and cysteine content.
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Studies on Synonymous Codon and Amino Acid Usage Biases in the Broad-Host Range Bacteriophage KVP40
Keya Sau,Sanjib Kumar Gupta,Subrata Sau,Subhas Chandra Mandal,Tapash Chandra Ghosh 한국미생물학회 2007 The journal of microbiology Vol.45 No.1
In this study, the relative synonymous codon and amino acid usage biases of the broad-host range phage, KVP40, were investigated in an attempt to understand the structure and function of its proteins/proteincoding genes, as well as the role of its tRNAs. Synonymous codons in KVP40 were determined to be ATrich at the third codon positions, and their variations are dictated principally by both mutational bias and translational selection. Further analysis revealed that the RSCU of KVP40 is distinct from that of its Vibrio hosts, V. cholerae and V. parahaemolyticus. Interestingly, the expression of the putative highly expressed genes of KVP40 appear to be preferentially influenced by the abundant host tRNA species, whereas the tRNAs expressed by KVP40 may be required for the efficient synthesis of all its proteins in a diverse array of hosts. The data generated in this study also revealed that KVP40 proteins are rich in low molecular weight amino acid residues, and that these variations are influenced primarily by hydropathy, mean molecular weight, aromaticity, and cysteine content.
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