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Analysis of seed proteome from wild and mutant lines of sorghum
Swapan Kumar Roy,Abu Hena Mostofa Kamal,Hye-Rim Kim,Soo-Jeong Kwon,Jung-In Kim,Tae-Seok Ko,Zhanguo Xin,Sun-Hee Woo 한국육종학회 2013 한국육종학회 심포지엄 Vol.2013 No.07
Grain sorghum (Sorghum bicolor) is a major staple for a large portion of the world. The crop ranks fifth among the cereals world-wide with respect to its importance for food and feed applications. To this end, the grain harvested from sorghum, and the millets provides an important source for dietary calories and protein for approximately one billion people in the semi-arid regions of the world. However, grain sorghum products are known to have relatively poor digestibility, only approximately 50%–70%, in comparison with other grains, such as wheat and maize, which tend to have digestibility percentages over 80% and 70%, respectively. Protein with high digestibility is by definition nutritionally superior owing to the increased availability of amino acids. Digestibility can be impacted by both protein–protein and⁄or protein–nonprotein interactions. However, with respect to grain sorghum, it is thought that the major factor influencing digestibility is the former because of high protein cross-linking around the protein body. To understand the mechanism of seed storage proteins in the sorghum, the proteomic analysis was carried out between the wild(BTX623) and mutant(M271207) genotypes of sorghum. Proteins were separated from the mature seed using IEF in the first-dimension and SDS-PAGE in the second dimension along with hybrid LTQ-FTICR mass spectrometry. After image analysis using Progenesis SameSpot software, we identified the 62 differential expressed protein spots out of 293 protein spots. Out of total differential expressed spots, 35 differential expressed protein spots (more than2-fold) were analyzed by mass spectrometry. Out of 35 protein spots, we were identified 20 protein spots as up-regulated and 15 protein spots as downregulated, significantly. In our proteomic investigation, the candidate proteins may provide novel clues for better understanding the characteristics of seed proteins in Sorghum.
명노준(No-Jun Myeong),최낙삼(Nak-Sam Choi),권현화(Hena Kwon) 대한기계학회 2013 대한기계학회 춘추학술대회 Vol.2013 No.12
An accelerated ultrasonic fatigue test(UFT) has been used for analyzing very high cycle fatigue( VHCF, N<SUB>f</SUB> > 10<SUP>7</SUP> ) behaviors. This study shows FEM results the dynamic behaviors of a specimen with a resonance of 20 kHz in UFT. The displacement and the stress along the specimen gage portion are calculated. The results are compared with those from the stress equation of the UFT specimen. The dynamic behavior of the gage portion was also visualized for the comparison with real images.
명노준(No-Jun Myeong),최낙삼(Nak-Sam Choi),권현화(Hena Kwon) 대한기계학회 2014 大韓機械學會論文集A Vol.38 No.7
본 논문에서는 초고주기피로영역의 가속시험 방법인 초음파 피로시험에 대해 20 kHz 근처에서 시험편 게이지부의 동적거동을 유한요소해석으로 검토하였다. 실제 실험에서 시험편에 작용하는 응력은 시험편의 형상과 변위를 통해 식으로 계산되는데 여기서 가정하는 시험편의 형상과 실제 시험편의 형상에 차이가 발생한다. 실험으로 구해진 응력과 유한요소 동적 해석의 결과를 비교하고 형상차이에 따른 응력분포를 확인하였다. 또한, 이론적으로 생각하는 초음파 피로시험기의 동적 거동을 가시적으로 확인하여 초음파 피로시험의 정확성을 확보하였다. An accelerated ultrasonic fatigue test (UFT) was used for analyzing very high cycle fatigue (VHCF, Nf > 107) behaviors of a specimen with a test resonance of 20 kHz. Using the finite element method (FEM), the dynamic behaviors of the specimen was studied by calculating the stresses along its gauge portion, with displacement. The shape of gauge portion profile was assumed to be a hyperbolic according to the stress equation of the UFT. However, as the specimen used in the test had a circular arc profile, the FEM was used for studying the local stresses for two cases of the gauge profile. The results were compared with those obtain from the stress equation of the UFT. The dynamic behavior of the gauge portion could be understood for further comparison with the actual results.