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조용식,전찬후 한국해안해양공학회 2003 한국해안해양공학회 논문집 Vol.15 No.2
본 연구에서는 Reynolds 방정을 지배방정식으로 하고 난류 해석을 위해 k-ε모델을 사용하였으며, 자유수면 변위를 추적하기 위해 VOF기법을 사용한 수치해석 모델을 이용하여 다양한 주기를 갖는 크노이드파의 발생과 최대 처오름높이에 대해 알아보았다. 발생된 크노이드파의 파형은 해석해와 매우 잘 일치하였다 또한, 계산된 최대 처오름높이를 수리모형실험의 관측 값과 비교해 본 결과는 경계요소법에 의한 수치해보다 높은 정확도를 나타내었다. This paper describes the generation and maximum run-up heights of cnoidal waves with varying periods by the numerical model. The model solves the Reynolds equations and the k-epsilon equations for the turbulent analysis. To track free surface displacements, the volume of fluid(VOF) method is employed. It is shown that profiles of the numerically generated cnoidal waves agree well with analytical solutions. The computed maximum run-up heights are compared with laboratory measurements and those of the boundary element method. The present model provides more agreeable results to laboratory measurements that the boundary element model.
자외선 조사가 Ovalbumin의 분자적 성질에 미치는 영향
조용식,송경빈,山田經路,한귀정 한국응용생명화학회 2008 Journal of Applied Biological Chemistry (J. Appl. Vol.51 No.4
To elucidate the effects of ultraviolet (UV) irradiation on molecular properties of ovalbumin, the molecular weight profile, secondary structure and tertiary structure of proteins were examined after irradiation by UV with 254 nm wavelength for 4, 8, 16 and 32 hrs, respectively. UV irradiation of protein solution caused the disruption on the native state of protein molecules. SDS-PAGE and gel permeation chromatography indicated that radiation caused initial fragmentation of polypeptide chains and as a result subsequent aggregation due to cross-linking of protein molecules. Circular dichroism (CD) study showed that UV irradiation caused the change on the secondary structure resulting in decrease of helical structure or compact denature on structure of protein depending on irradiation period. Fluorescence spectroscopy indicated that irradiation quenched the emission intensity excited at 280 nm. These results suggest that UV irradiation affect the molecular properties of ovalbumin and may have potential as a means to change the antigenicity of protein allergen. To elucidate the effects of ultraviolet (UV) irradiation on molecular properties of ovalbumin, the molecular weight profile, secondary structure and tertiary structure of proteins were examined after irradiation by UV with 254 nm wavelength for 4, 8, 16 and 32 hrs, respectively. UV irradiation of protein solution caused the disruption on the native state of protein molecules. SDS-PAGE and gel permeation chromatography indicated that radiation caused initial fragmentation of polypeptide chains and as a result subsequent aggregation due to cross-linking of protein molecules. Circular dichroism (CD) study showed that UV irradiation caused the change on the secondary structure resulting in decrease of helical structure or compact denature on structure of protein depending on irradiation period. Fluorescence spectroscopy indicated that irradiation quenched the emission intensity excited at 280 nm. These results suggest that UV irradiation affect the molecular properties of ovalbumin and may have potential as a means to change the antigenicity of protein allergen.