• 한국지구과학회:학술대회논문집
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• 2006.02a
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• pp.230-234
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• 2006

본 연구에서는 미분화 운석 중 오디너리 콘드라이트를 주사전자 현미경으로 관찰하여 열변성, 충격 변성 정도, 지구상에서의 풍화 정도에 따라서 그 구성 성분과 조직이 어떤 변화를 보이는지 알아보았다. 이를 위해 15개의 오디너리 콘드라이트에 대해 각각 연마편 및 연마박편을 준비하였으며, 주사전자 현미경 사진을 이용하여 열변성 단계별로 콘드률과 기질의 경계를 비교하였다. 열변성이 증가할수록 콘드률과 기질의 경계는 점차 모호해 진다. 충격변성을 받았는지의 유무는 감람석을 관찰하여 비교적 쉽게 인지할 수 있다. 충격변성을 받지 않은 콘드률 내의 감람석은 완전 소광과 불규칙적인 깨짐을 보이지만 충격변성을 받은 경우 파동소광과 규칙적인 깨짐을 보인다. 지구상에서 풍화를 받은 경우 철-니켈 금속의 산화가 가장 먼저 진행된다. 풍화에 의한 철산화물은 맥상으로 나타나거나 기존의 철-니켈 금속을 치환하여 나타난다. 철산화물에 의해 풍화를 받은 콘드라이트는 전체적으로 갈색을 띄게 된다.

• The Korean Journal of Pharmacology
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• v.32 no.3
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• pp.433-444
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• 1996

We describe a novel approach to evaluate quantitatively the amounts of denatured proteins in cells upon heat exposure. A thiol compound, diamide [azodicarboxylic acid bis (dimethylamide)] causes protein cross-linking with exposed sulfyhydryl residues of denatured proteins. Since denatured proteins expose normally well-hidden sulfhydryl groups, these will be preferentially cross-linked by diamide. Thus diamide acts to 'trap' denatured proteins. We observed that protein aggregates (high molecular weight protein aggregates, HMA) appeared on SDS-polyacrylamide gels run under non-reducing conditions and that the amount of HMA can be quantified by scanning the gels using a gas flow counter. Heating cells followed by a fixed dose of diamide exposure resulted in HMA increases in a heat-dose dependent manner, demonstrating that the quantitation of HMA could serve as a measure of heat-denatured proteins. We compared thermotolerant and nontolerant cells and found decreased HMA in tolerant cells upon heat treatment. As an attempt to examine the kinetics of protein renaturation (or 'repair'), we measured the amounts of aggregates formed by the addition of diamide at various times after heat shock. Such experiments demonstrate an equally rapid disappearance of HMA in previously unheated and in thermotolerant cells. Levels of HMA in tolerant cells increased significantly after electroporation of HSP70 specific mAbs, suggesting an involvement of HSP70 in reducing HMA levels in thermotolerant cells upon heat exposure. Immunoprecipitation studies using anti-HSP70 antibody indicated an association of HSP70 with heat-denatured proteins. Our results suggest that heat induces protein denaturation, and that elevated level of HSP70 present in thermotolerant cells protects them by reducing the level of protein denaturation rather than by facilitating the 'repair' (or degradation) process.

• The Journal of the Petrological Society of Korea
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• v.19 no.4
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• pp.255-267
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• 2010

The primary utilization of recently improved (U-Th)/He thermochronometry is to reveal the low-T thermal histories of shallow crustal sections or transient episodes (such as wildfires or meteorite impacts) because of the high sensitivity of He diffusion to temperature in host minerals. In this contribution, we present reviews and perspectives regarding how this method can be used to characterize the ejection-related shock metamorphism of Martian meteorites. The temperature conditions of shock metamorphism can be constrained through shock recovery experiments, paleomagnetism, and $^{40}Ar/^{39}Ar$ and (U-Th)/He dating. The most reliable constraints can be deduced when these independent approaches are combined. However, the thermal history of the ALH84001 Martian meteorite has been under serious debate because the different methods have yielded contrasting results. Recent work has shown how single-grain (U-Th)/He and $^{40}Ar/^{39}Ar$ dating, two noble-gas based thermochronometries with different T sensitivities, can be used to resolve this issue, providing a good example for future research on other meteorites.