• 제목/요약/키워드: Unfolded Surface

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선박 외판 성형에서 목적 형상과 전개 평판의 최적 정합을 위한 ICP(Iterative Closest Point) 알고리즘 적용 (Application of ICP(Iterative Closest Point) Algorithm for Optimized Registration of Object Surface and Unfolding Surface in Ship-Hull Plate Forming)

  • 이장현;윤종성;류철호;이황범
    • 한국CDE학회논문집
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    • 제14권2호
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    • pp.129-136
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    • 2009
  • Generally, curved surfaces of ship hull are deformed by flame bending (line heating), multi-press forming, and die-less forming method. The forming methods generate the required in-plane/bending strain or displacement on the flat plate to make the curved surface. Multi-press forming imposes the forced displacements on the flat plate by controlling the position of each pressing points based upon the shape difference between the unfolded flat plate and the curved object shape. The flat plate has been obtained from the unfolding system that is independent of the ship CAD. Apparently, the curved surface and the unfolded-flat surface are expressed by different coordinate systems. Therefore, one of the issues is to find a registration of the unfolded surface and the curved shape for the purpose of minimum amount of forming works by comparing the two surfaces. This paper presents an efficient algorithm to get an optimized registration of two different surfaces in the multi-press forming of ship hull plate forming. The algorithm is based upon the ICP (Iterative Closest Point) algorithm. The algorithm consists of two iterative procedures including a transformation matrix and the closest points to minimize the distance between the unfolded surface and curved surfaces. Thereby the algorithm allows the minimized forming works in ship-hull forming.

Ubiquitin 폴딩 intermediate의 열역학적 특성 (Thermodynamic Properties of Ubiquitin Folding Intermediate)

  • 박순호
    • Applied Biological Chemistry
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    • 제47권1호
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    • pp.33-40
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    • 2004
  • Ubiquitin 폴딩 반응의 초기에 나타나는 transient 폴딩 intermediate 상태의 열역학적인 특성을 연구하였다. 온도와 화학변성제의 농도를 바꾸어주면서 측정한 폴딩 kinetics의 결과로부터 unfolded 상태와 intermediate 상태의 평형상수 및 자유에너지를 quantitative kinetic modeling을 통하여서 구하였으며 또한 온도에 따른 자유에너지의 변화로부터 unfolded 상태에서 intermediate 상태로 전환될 때의 열역학적 함수인 ${\Delta}H,\;{\Delta}S,\;{\Delta}C_p$를 구하였다. Ubiquitin이 unfolded 상태에서 intermediate 상태가 될 때의 ${\Delta}C_p$는 unfolded 상태에서 native 상태로 되는 과정의 ${\Delta}C_p$의 약 80% 정도 되었다. 이것은 intermediate가 native 상태에 가까운 매우 조밀한 구조를 이루고 있는 ensemble state임을 나타낸다. 상온에서의 ${\Delta}H$는 양의 값을 보였다. 이는 ubiquitin의 unfolded 상태에서 소수성 잔기 주위에 위치한 물 분자의 규칙적인 구조가 intermediate 상태가 될 때 와해되기 때문이라고 여겨진다. 이러한 양의 enthalpy는 자유로워진 물 분자에 의한 전체 계의 entropy의 증가에 의하여서 보상되어 unfolded 상태에서intermediate 상태로의 전환은 음의 자유에너지를 갖게 되며 폴딩 반응의 초기에 관찰되는 것으로 여겨진다.

A Kinetic Study on the Adsorptionof Compact, Water-soluble Proteins onto Aqueous Surfaces

  • 조태철;Michel A. Cornec
    • Bulletin of the Korean Chemical Society
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    • 제20권9호
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    • pp.999-1004
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    • 1999
  • Two compact sized globular proteins, β-lactoglobulin and α-lactalbumin were kinetically characterized at the aqueous solution surface with the measurement of surface pressure (π) and surface concentration (Γ) via a radiotracer method. The adsorption kinetics was of diffusion control at early times, the rates of increase of πand Γ being lower at longer times due to growing energy barrier. At low concentrations, an apparent time lag was observed in the evolution of π for β-lactoglobulin but not for α-lactalbumin which was shown to be due to the non-linear nature of the p- G relationship for the former. The area per molecule of an adsorbed β-lactoglobulin during adsorption was smaller than that for spread monolayer since β-lactoglobulin was not fully unfolded during the adsorption. For α-lactalbumin, however, no such difference in the molecular areas for adsorbed and spread monolayer was observed indicating thereby that α-lactalbumin unfolded much more rapidly (has looser tertiary structure) than β-lactoglobulin. Surface excess concentrations of α-lactalbumin was found to evolve in two steps possibly due to the change in the orientation of the adsorbed protein from a side-on to an end-on orientation.

Unfolded Histidine-Tagged Protein is Immobilized to Nitrilotriacetic Acid-Nickel Beads, But Not the Nickel-Coated Glass Slide

  • Cho Min-Ho;Ahn Sun-Young;Park Heon-Yong
    • Genomics & Informatics
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    • 제4권3호
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    • pp.133-136
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    • 2006
  • The adsorption of proteins on the surface of glass slides is essential for construction of protein chips. Previously, we prepared a nickel-coated plate by the spin-coating method for immobilization of His-tagged proteins. In order to know whether the structural factor is responsible for the immobilization of His-tagged proteins to the nickel-coated glass slide, we executed a series of experiments. First we purified a His-tagged protein after expressing the vector in E. coli BL21 (DE3). Then we obtained the unfolding curve for the His-tagged protein by using guanidine hydrochloride. Fractions unfolded were monitored by internal fluorescence spectroscopy. The ${\Delta}G_{H20}$ for unfolding was $2.27kcal/mol{/pm}0.52$. Then we tested if unfolded His-tagged proteins can be adsorbed to the nickel-coated plate, comparing with $Ni^{2+}-NTA$ (nitrilotriacetic acid) beads. Whereas unfolded His-tagged proteins were adsorbed to $Ni^{2+}-NTA$ beads, they did not bind to the nickel-coated plate. In conclusion, a structural factor is likely to be an important factor for constructing the protein chips, when His-tagged proteins will immobilize to the nickel-coated slides.

Mitoxantrone Binds to Nopp140, an Intrinsically Unstructured Protein, and Modulate its Interaction with Protein Kinase CK2

  • Lee, Won-Kyu;Lee, Sang-Yeop;Na, Jung-Hyun;Jang, Sung-Woo;Park, Chan-Ryang;Kim, Soo-Youl;Lee, Si-Hyeong;Han, Kyou-Hoon;Yu, Yeon-Gyu
    • Bulletin of the Korean Chemical Society
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    • 제33권6호
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    • pp.2005-2011
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    • 2012
  • Nopp140 is a highly phosphorylated protein that resides in the nucleolus of mammalian cell and is involved in the biogenesis of the nucleolus. It interacts with a variety of proteins related to the synthesis and assembly of the ribosome. It also can bind to a ubiquitous protein kinase CK2 that mediates cell growth and prevents apoptosis. We found that Nopp140 is an intrinsically unfolded protein (IUP) lacking stable secondary structures over its entire sequence of 709 residues. We discovered that mitoxantrone, an anticancer agent, was able to enhance the interaction between Nopp140 and CK2 and maintain suppressed activity of CK2. Surface plasma resonance studies on different domains of Nopp140 show that the C-terminal region of Nopp140 is responsible for binding with mitoxantrone. Our results present an interesting example where a small chemical compound binds to an intrinsically unfolded protein (IUP) and enhances protein-protein interactions.

수용성 단백질의 계면상 등온곡선의 모델과 실험적 규명 (Model and Experimental Isotherms of Soluble Proteins at water sur faces)

  • Cho, D.
    • 한국산학기술학회:학술대회논문집
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    • 한국산학기술학회 2003년도 춘계학술발표논문집
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    • pp.328-330
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    • 2003
  • A surface equation of state for globular proteins at air-water interface accounting for the molecular structure, segment-segment, segment-solvent, and electrostatic interactions was proposed and compared to C-14 isotope experiments. This lattice model comprised a simplifying assumption that all adsorbed segments are in the form of trains. The number of segment adsorbed per molecule in case of bovine serum albumin linearly depended on the surface concentration whereas the lysozyme segments adsorbed at the interface were independent of surface concentration. The segment-solvent(water) interaction for both of proteins were found to be unfavorable owing to the proteins unfolding. From comparison of model computation and experimental data, BSA unfolded more than lysozyne because of the larger surface area of contact.

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유비퀴틴 단백질의 부분적으로 폴딩된 구조에 대한 분광학적 분석 (Spectroscopic Analysis of Partially Folded State of Ubiquitin)

  • 박순호
    • Applied Biological Chemistry
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    • 제46권4호
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    • pp.305-310
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    • 2003
  • Hydrophobic core가 변이된 유비퀴틴 단백질이 pH 2 용액에서 보이는 구조적인 특성을 여러 분광학적 방법으로 측정하였다. 낮은 pH값을 갖는 용액에서 이 변이 유비퀴틴의 intrinsic tryptophan fluorescence emission spectrum은 unfolded 상태보다 약간 blue shift되어 있고 또한 그 intensity도 상당히 낮게 나타났다. 이는 이 용액 조건에서 이 변이 유비퀴틴의 삼차구조가 약간 남아 있는 것을 의미한다. 같은 용액에서 이 변이 유비쥐틴의 far-UV circular dichroic spectrum은 native 상태나 unfolded 상태의 spectrum과 현저히 달랐으며 220 nm 에서의 molar ellipticity 값을 통하여 볼 때 pH 2인 용액에서 상당량의 이차구조를 지니고 있었다. 또한 같은 용액에서 이 변이 유비퀴틴은 hydrophobic dye인 8-anilinonaphthalene-1-sulfonic acid(ANS)외 fluorescence emission intensity를 증가시키고 fluorescence emission maximum이 짧은 파장에서 나타나게 하였다(blue shift). 이러한 현상은 pH 2 용액에서 이 변이 유비퀴틴의 hydrophobic core가 느슨하여져서 hydrophobic dye인 ANS가 결합할 수 있는 구조를 띠고 있음을 나타낸다. 이러한 분광학적인 관찰은 이 변이 유비귀틴이 pH 2인 용액에서 상당량의 이차구조를 지니고 있지만 hydrophobic core는 느슨하게 형성된 molten globule과 같은 형태를 지니고 있음을 나타낸다. 이 변이 유비퀴틴의 molten 히obule 형태는 단백질 폴딩 반응의 경로를 연구할 수 있는 좋은 모델이 될 수 있을 것으로 생각된다.

3D 동체 모형을 이용한 2D 전개 패턴 연구 (2D Flat Pattern Development Using Simplified 3D Torso Model)

  • 김명수;홍경희
    • 대한인간공학회지
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    • 제24권2호
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    • pp.85-91
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    • 2005
  • To understand the basic relationship between 3D curved surface model and 2D pattern, simplified torso model was generated by commercial CAD program (IDEAS). 3D torso model was then divided into different blocks and unfolded into a flat pattern as in ordinary works of clothing item design. As results, 2D pattern development of different part of 3D torso model was attempted and analyzed mathematically. It was found that different height, radius and tangent slope of 3D blocks resulted in different 2D pattern. The relationships between the shape parameters of 3D torso blocks and those of 2D patterns were analyzed using regression equations. Direct way of drawing a 2D pattern of corresponding 3D torso block was also illustrated for the convenience of pattern making using conventional measurements of upper/ lower radii and height of 3D torso block.

스포츠댄스용 연미복의 Prototype에 관한 연구 (A Study on the Prototype of Swallow-tailed Coat for Sports Dance)

  • 오영순;김여숙
    • 한국의류산업학회지
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    • 제8권4호
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    • pp.433-440
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    • 2006
  • This research was made to suggest a functional and fitted prototype of swallow-tailed coat for sports dance. We established the basic posture of standard dance from literature investigations, and grasped the changes of the body side-surface by motions through the gypsum-experiments with a man in twenty. The unfolded gypsum shells were overlapped on the basic swallow-tailed coats pattern drafted by their size of experimenter. From our results through analysis, our pattern of the swallow-tailed coats for sports dance was designed considering their functional and structural character. In case of upper body with the greatly increased shoulder width of garment and with the decreased front. When moving, owing to the rising of the armpit point, the side-line becomes longer with the shoulder length decreased greatly. In case of sleeves, the length of sleeves back increased greatly by the arm-bending motions while sleeve height becomes lowered.

Shell Template Offset 도면을 활용한 선체 곡판 형상 복원 방법에 관한 연구 (A Study on the Method for Reconstructing the Shell Plates Surface from Shell Template Offset Drawing)

  • 황인혁;손승혁
    • 대한조선학회논문집
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    • 제56권1호
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    • pp.66-74
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    • 2019
  • In the field of shipbuilding design, the use of 3D CAD is becoming commonplace, and most of the large shipyards are conducting 3D design. However at the production site, workers are still working on 2D drawings rather than 3D models. This tendency is even worse in small-scale shipyards and block manufacturing shops. Particularly, in a manufacturing shop that is engaged in the outsourcing of blocks, it may not be possible to provide 3D model. However, the demand for 3D models in the production field is steadily increasing. Therefore, it would be helpful if 3D model could be generated from a 2D drawing. In this paper, we propose a method to extract template and unfolded surface shape information from shell template offset drawing using computer vision technology. Also a 3D surface model was reconstructed and visualized from the extracted information. The result of this study is thought to be helpful in the work environment where 3D model information can not be obtained.