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 thepressure
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
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