| 학회 | 한국화학공학회 |
| 학술대회 | 1998년 가을 (10/23 ~ 10/24, 조선대학교) |
| 권호 | 4권 2호, p.2885 |
| 발표분야 | 분체공학 |
| 제목 | 패각의 결정내부단백질 2차구조의 정량적 해석 |
| 초록 | Aragonite and calcite are the two carbonate skeletons most frequently encountered in biological systems. These biogenic minerals have the unique mineralogy quite different fromthose found in nonbiological precipitates[1]. It is known that CaCO3 polymorphs constitute 98to 99% of the inorganic material of oyster shells. Also it was reported that aragonite wasformed easily from a solution at a temperature above 50℃. It is likely to more easily inducethe nucleation of the thermodynamically more stable polymorph calcite[2]. The aragonite,however, has been readily found in the deposited minerals.A number of experiments have been made to inspect the mechanisms of inorganiccrystallization at mineralized tissue. The biological approaches have been to isolate theprotein components from organisms and examine the formation of calcium salts in thepresence of these components[3]. The difficulty with these studies is that the exact nature ofthe interaction between the minerals and the shell proteins is not well understood. One majorreason is the difficulty of analyzing biomineralization processes in their native state[4].Biomimetic systems have indicated the importance of electrostatic binding or association,geometric matching(epitaxis), and stereochemical correspondence at inorganic-organicinterfaces. Although these methods appear to be plausible, they have not provided adequateexplanations for the oriented crystallization in biological systems. Yet we have littleunderstanding of crystal science in terms of bonding and reactivity of organized structures.In this paper, in order to explain the mineral-specific proteins we could assume thatoyster secretes one particular calcifying protein to form a specific layer and calcium ions arebinding to the COO- groups of amino acid side chains inside these proteins. And toquantitatively investigate the secondary structure of mineral-specific proteins, resolutionenhancement techniques, such as Fourier self deconvolution and gaussian curve-fittingtechniques were applied. If either the α-helix or β-sheet content in a given system ishigher or lower than that of the native form, it could be thought that it is demonstrating thedisordering and rearrangement of secondary structure. Also we are to obtain new informationon the interaction between calcium ions and mineral-specific proteins. The results show themethods for understanding the principles that govern shell formation, and the insight into themechanisms by which these shell protein constituents control crystal polymorph in vivo. |
| 저자 | 김용완, 윤은선, 최청송 |
| 소속 | 서강대 |
| 키워드 | FTIR; INTRACRYSTALLINE PROTEIN; POLYMORPH |
| 원문파일 | 초록 보기 |
