学会誌「高圧力の科学と技術」
Rev. High Pressure Sci. Technol.

Vol.10  No.2 (2000) Abstract


特集−生体高分子−
Rev. High Pressure Sci. Technol. 10-2,88-94(2000)
高圧NMRによる蛋白質研究の新しい展開
―広い構造アンサンブルの探索―
High Pressure NMR Enabling a Wide Conformational Search of Proteins
赤坂一之
Kazuyuki AKASAKA
Many proteins are considered to perform their functions by dynamic excursion to "other" conformations that deviate from the basic structure found in crystal. These "other" conformations have seldom become targets of detailed structural study. The on-line cell high pressure NMR technique developed at Kobe is the only available technique capable of producing "other" conformations of proteins and simultaneously reporting their structures at residue-specific resolution using multi-dimensional NMR spectroscopy. The principle is based on the recognition that the partial molar volume of a protein strongly depends on its conformational state. Examples are given from two proteins, basic pancreatic trypsin inhibitor and the Ras-binding domain of RalGEF.

[high pressure NMR, partial molar volume, protein conformation, pressure denaturation, local unfolding, multi-dimensional NMR, structural fluctuation, conformational ensemble]
〒657-8501 神戸市灘区六甲台町1-1 神戸大学大学院自然科学研究科分子集合科学専攻
Department of Molecular Science, Graduate School of Science and Technology, Kobe University 1-1 Rokkodai-cho, Nada-ku, Kobe 657-8501



特集−生体高分子−
Rev. High Pressure Sci. Technol. 10-2,95-100(2000)
高圧赤外分光法によるタンパク質の研究における最近の進展
Recent Advances in High-Pressure Infrared Spectroscopic Studies on Proteins
スボラック ボイチェク・加藤 稔・谷口吉弘
Wojciech DZWOLAK Minoru KATO Yoshihiro TANIGUCHI
This paper aims to review recent trends and developments in high-pressure FTIR studies on proteins. Methodological principles of research in this field, the assignment of the diagnostically-useful IR bands, as well as several examples illustrating the application of IR spectroscopy in high pressure studies on proteins are all within the scope of this article. This work is also an attempt to show that IR spectroscopy can find application not only for studies of the pressure-induced unfolding of protein structure, but also for the examination of minor unfolding events or local conformational changes induced by high pressure. A more elaborate discussion of the high-pressure study on bovine a-lactalbumin is also presented.

[DAC, proteins under high pressure, unfolding, IR spectroscopy, H/D-exchange]
〒525-8577 滋賀県草津市野路東1-1-1 立命館大学理工学部応用化学科 
Department of Applied Chemistry, College of Science and Engineering, Ritsumeikan University, 1-1-1 Nojihigashi, Kusatsu, Shiga 525-8577



特集−生体高分子−
Rev. High Pressure Sci. Technol. 10-2,101-107(2000)
蛋白質の圧縮率と立体構造
Compressibility-Structure Relationship of Proteins
月向 邦彦
Kunihiko GEKKO
Protein dynamics is a basis for understanding the principles of constructing three-dimensional structures and the structure-function relationship of proteins. A novel measure of the flexibility of protein in water is compressibility because it is directly linked to the volume fluctuation. It is known that the adiabatic compressibility sensitively reflects the structural characteristics of proteins although it is a thermodynamic quantity. This article is a review of recent studies on the compressibility-structure relationship of native globular proteins.

[adiabatic compressibility, flexibility, protein structure, cavity, hydration]
〒739-8526 東広島市鏡山1-3-1 広島大学大学院理学研究科
Graduate School of Science, Hiroshima University, Kagamiyama 1-3-1, Higashi-Hiroshima 739-8526



特集−生体高分子−
Rev. High Pressure Sci. Technol. 10-2,108-115(2000)
高圧力下の酵素反応
Enzyme Reaction under High Pressure
巻本 彰一
Syoichi MAKIMOTO
From the many studies in enzyme reactions under high pressure, the activation volume for the catalytic process and the reaction volume for the dissociation process of the Michaelis complex evaluated from the pressure dependence of the enzyme reaction are found to be powerful tools for studying the reaction mechanisms in these processes. The above volume changes not only clarify the enzyme reaction mechanism, but also may explain the relationship between the high catalytic efficiency/specificity and the reactionmechanism. As an example of an enzyme reaction, the reaction mechanism of α-chymotrypsin(α-CHT) catalysis is discussed in terms of the volume change.

[pressure; enzyme reaction; reaction volume; activation volume; α-chymotrypsin]
〒612-8522 京都市伏見区深草藤森町1 京都教育大学教育学部理学科
Department of Science, Faculty of Education, Kyoto University of Education, 1 Fukakusafujinomori-cho, Fushimi-ku,Kyoto 612-8522



特集−生体高分子−
Rev. High Pressure Sci. Technol. 10-2,116-123(2000)
高圧力による酵素反応生成物の制御
Control of Products for the Enzyme Reaction by High Hydrostatic Pressure
松本 正 巻本 彰一*  谷口 吉弘**
Tadashi MATSUMOTO Syoichi MAKIMOTO Yoshihiro TANIGUCHI
To investigate the possibility that pressure can control the products for the enzyme reactions, pressure effects on the time course of the products' composition accompanying the hydrolysis of maltooligosaccharides[maltotetraose (G4), maltopentaose (G5), and maltohexaose (G6)] and amylose catalyzed by porcine pancreatic α-amylase (PPA) were measured up to 300 MPa at 30℃. The composition of products for the hydrolysis of G5 substrates changed slightly by compression. But for G4, G6 and amylose substrate, pressure induced some changes in the composition of the products. These results tell us that pressure is one of the efficacious tools to control the products of enzyme reaction of α-amylase. The mechanism of an interesting pressure-induced reaction catalyzed by PPA is discussed in terms of the volume differences among enzyme-substrate (ES) complexes.

[pressure, control of enzyme reaction, porcine pancreatic α-amylase, maltooligosaccharides, amylose, volume difference]
〒520-3004 栗太郡栗東町上砥山232 滋賀県工業技術総合センター技術第2科
Industrial Research Center of Shiga Prefecture, 232 Kamitoyama, Ritto, Shiga 520-3004
* 〒612-8522 京都市伏見区深草藤森町1京都教育大学教育学部理学科
Department of Science, Faculty of Education, Kyoto University of Education, 1 Fukakusafujinomori-cho, Fushimi-ku, Kyoto 612-8522
** 〒525-8577 草津市野路東1-1-1 立命館大学理工学部化学科
Department of Chemistry, Collage of Science and Engineering, Ritsumeikan University, 1-1-1 Nojihigashi, Kusatsu-city, Shiga 525-8577



解説
Rev. High Pressure Sci. Technol. 10-2,124-133(2000)
地球内部の水  -マントル遷移層は水のリザバーか?-
Water in the Earth's interiors -Is the mantle transition zone a water reservoir?-
井上 徹
Toru INOUE
H2O is an important volatile material in the Earth, and it affects the physical properties (e.g. density, elastic velocity, viscosity, rheological property, diffusion, electrical conductivity and melting temperature) of the Earth's materials. Recently, it has been clarified that significant amounts of H2O can be accommodated in β and γ phases of olivine, which means that the mantle transition zone has the potential of being a water reservoir in the Earth. In this paper, I review the H2O contents, lattice parameters and elastic properties of hydrous β and γ phases, the effect of H2O on the phase transformation of olivine, and the possibilities of water transportation into the mantle transition zone are discussed on the basis of these experimental data.

[water, hydrous phases, olivine, mantle transition zone, hydrous wadsleyite, hydrous ringwoodite]
〒790-8577 愛媛県松山市文京町2-5愛媛大学理学部生物地球圏科学科
Department of Earth Sciences, Ehime University, Bunyo-cho 2-5, Matsuyama 790-8577, Ehime, Japan



解説
Rev. High Pressure Sci. Technol. 10-2,134-141(2000)
第一原理計算を用いた高圧下の未知構造及び物性探索
First-Principles Investigation of Unknown Structures and
Properties of Materials under Pressure
館山 佳尚
Yoshitaka TATEYAMA
The constant-pressure first-principles molecular dynamics (CP-FPMD) method shows its great power in the investigation of high-pressure phenomena which are difficult to observe in experiments. In this article, I present a survey of this CP-FPMD method as well as a new technique we developed for the determination of transition states. I also illustrate their ability with our inviestigations of high-pressure sysntesis of BCN heterodiamondsands and pressure induced metallization of organic monomolecular crystals.
[ first-principles calculation, constant-pressure scheme, structural transformation, transition state, electronic state, metallization]
〒305-0047 茨城県つくば市千現1-2-1 科学技術庁 金属材料技術研究所
National Research Institute for Metals, 1-2-1 Sengen, Tsukuba-shi, Ibaraki 305-0047




〒606-0805
京都市左京区下鴨森本町 15 (財)生産開発科学研究所内
日本高圧力学会事務局
Tel (075)721-0376 Fax (075)723-9629
koatsu@mbox.kyoto-inet.or.jp