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CGI 소프트웨어를 기반으로 한 파라메트릭 건축 디자인의 형태 형성 프로세스에 관한 연구 KCI 등재
대한건축학회지회연합회 대한건축학회연합논문집 제16권 제6호 통권 64호 2014.12 pp.11-18
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최근 파라메트릭 디자인은 디지털 테크닉과 컴퓨테이션에 기반을 둔 건축 프로젝트에서 지배적으로 나타나는 형식이 되었다. 파라메트릭 디자인에서 새로운 건축 형태 생성의 잠재력이 반드시 건축 디자인을 위해서 개발된 전통적인 CAD 소프트웨어만을 통해서만 탐구되는 것은 아니다. 원래는 영화나 애니메이션 산업을 위하여 개발된 CGI 소프트웨어들이 파라메트릭 디자인 원리를 구현하는 훌륭한 대안으로 인식되고 있다. 이 연구에서는 파라메트릭 형태 형성 과정에 사용되는 여러 디지털 애니메이션 소프트웨어의 테크닉들이 논의되며, 이 테크닉들이 건축 디자인에 어떻게 영향을 주어 엘레간스의 가치를 실현시키기 위해 도움을 주었는지 분석한다.
Parametric design has become the most dominant style among the most recent architectural projects based on digital techniques and computation. Its potential for generating new architectural form is not always explored by using conventional CAD software intended for architectural design. CGI(Computer-Generated Imagery) Software originally developed for film and animation industry are recognized as a strong alternative way of realizing parametric design principles. In this study, various techniques of digital animation software for parametric form-finding process are discussed and how these techniques influence parametric architectural design to help achieving elegance is analyzed.
[Kisti 연계] 대한구강생물학회 International journal of oral biology Vol.42 No.2 2017 pp.71-78
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BMP-2 is a well-known TGF-beta related growth factor, having a significant role in bone and cartilage formation. It has been employed to promote bone formation in some clinical trials, and to differentiate mesenchymal stem cells into osteoblasts. However, it is difficult to obtain this protein in its soluble and active form. hBMP-2 is expressed as an inclusion body in the bacterial system. To continuously supply hBMP-2 for research, we optimized the refolding of recombinant hBMP-2 expressed in E. coli, and established an efficient method by using detergent and alkali. Using a heparin column, the recombinant hBMP-2 was purified with the correct refolding. Although combinatorial refolding remarkably enhanced the solubility of the inclusion body, a higher yield of active dimer form of hBMP-2 was obtained from one-step refolding with detergent. The refolded recombinant hBMP-2 induced alkaline phosphatase activity in mouse myoblasts, at $ED_{50}$ of 300-480ng/ml. Furthermore, the expressions of osteogenic markers were upregulated in hPDLSCs and hDPSCs. Therefore, using the process described in this study, the refolded hBMP-2 might be cost-effectively useful for various differentiation experiments in a laboratory.
[NRF 연계] 대한구강생물학회 International Journal of Oral Biology Vol.42 No.2 2017.06 pp.71-78
※ 협약을 통해 무료로 제공되는 자료로, 원문이용 방식은 연계기관의 정책을 따르고 있습니다.
BMP-2 is a well-known TGF-beta related growth factor, having a significant role in bone and cartilage formation. It has been employed to promote bone formation in some clinical trials, and to differentiate mesenchymal stem cells into osteoblasts. However, it is difficult to obtain this protein in its soluble and active form. hBMP-2 is expressed as an inclusion body in the bacterial system. To continuously supply hBMP-2 for research, we optimized the refolding of recombinant hBMP-2 expressed in E. coli, and established an efficient method by using detergent and alkali. Using a heparin column, the recombinant hBMP-2 was purified with the correct refolding. Although combinatorial refolding remarkably enhanced the solubility of the inclusion body, a higher yield of active dimer form of hBMP-2 was obtained from one-step refolding with detergent. The refolded recombinant hBMP-2 induced alkaline phosphatase activity in mouse myoblasts, at ED50 of 300-480ng/ml. Furthermore, the expressions of osteogenic markers were upregulated in hPDLSCs and hDPSCs. Therefore, using the process described in this study, the refolded hBMP-2 might be cost-effectively useful for various differentiation experiments in a laboratory.
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