著者
西坂 崇之 政池 知子
出版者
一般社団法人 日本生物物理学会
雑誌
生物物理 (ISSN:05824052)
巻号頁・発行日
vol.47, no.2, pp.118-123, 2007 (Released:2007-03-31)
参考文献数
18

F1-ATPase is a rotary molecular motor in which unidirectional rotation of the central γ-subunit is powered by ATP hydrolysis in three catalytic sites arranged 120° apart around γ. To see how hydrolysis reactions produce mechanical rotation, we observed rotation of γ under the optical microscope, while watching which of the three sites bound and released a fluorescent ATP analog. The reaction scheme, including both the number of site occupancy and reactions that trigger substeps, is now established.
著者
有本 理恵子
出版者
一般社団法人日本生物物理学会
雑誌
生物物理 (ISSN:05824052)
巻号頁・発行日
vol.38, no.6, pp.264-266, 1998-11-01
参考文献数
8
著者
井上 豪 裏出 良博
出版者
一般社団法人 日本生物物理学会
雑誌
生物物理 (ISSN:05824052)
巻号頁・発行日
vol.47, no.1, pp.036-043, 2007 (Released:2007-02-21)
参考文献数
22

The structural based drug-design (SBDD) is one of the useful methods for producing a novel medicine. We recently succeeded in X-ray crystallographic determination of two target molecules. One is human hematopoietic prostaglandin (PG) D synthase (H-PGDS) that produces PGD2 as an allergic mediator in mast cells and Th2 cells. The other is Trypanosoma brucei PGF2α synthase (TbPGFS), a member of the aldo-ketoreductase superfamily, catalyzes the NADPH-dependent reduction of PGH2 to PGF2α, whose overproduction during trypanosomiasis causes miscarriage in infected female subjects. In this report, we introduce the recent progress in the research of the high resolution structures of human H-PGDS and TbPGFS useful for SBDD.
著者
田口 英樹
出版者
一般社団法人 日本生物物理学会
雑誌
生物物理 (ISSN:05824052)
巻号頁・発行日
vol.46, no.3, pp.130-136, 2006 (Released:2006-05-25)
参考文献数
27
被引用文献数
1 1

The chaperonin GroEL is an essential molecular chaperone that assists protein folding in the cell. ATP-dependent conformational change of GroEL leads to the stable binding of cochaperonin GroES, forming a cage-shaped complex that accommodates a substrate protein to complete the folding. After the elucidation of the outline of the molecular mechanism over the last decade, now we are ready to answer the important questions; how GroEL encapsulate the substrate protein? How the substrate protein influences the functional cycle of GroEL? What is the role of ATP hydrolysis in the GroEL-assisted folding? Is the folding in the GroEL-ES cavity is same as that in the bulk solution? Here I review the recent progress on the GroEL study and discuss the essential role of chaperonin GroEL.
著者
古瀬 幹夫
出版者
一般社団法人日本生物物理学会
雑誌
生物物理 (ISSN:05824052)
巻号頁・発行日
vol.40, no.4, pp.229-233, 2000-07-25

Tight junctions, the most apical component of intercellular junctions, play pivotal roles in epithelial barrier by sealing the intercellular space. Very recently claudins were identified as the major molecular components of tight junction. Claudins not only work as adhesion molecules but also form tight junction strands probably by their polymerizing activity in the plasma membranes. Identification of claudins has enabled us to examine the molecular mechanism of epithelial barrier and permeability.
著者
矢野 雅文 三浦 治己
出版者
一般社団法人 日本生物物理学会
雑誌
生物物理 (ISSN:05824052)
巻号頁・発行日
vol.39, no.5, pp.306-311, 1999-09-25 (Released:2000-04-12)
参考文献数
9
被引用文献数
1

It is assumed that positional information within a developing organism is represented by a morphogen gradient. However, it is not yet understood how positional information is organized in a size invariant manner. To achieve such size invariance, it is necessary for an organism to organize the polarity of positional information in advance. We focus on tactic behavior of the Physarum plasmodium and propose a model that describes the organization of size invariant positional information, in which the direction of the phase wave represents the polarity. We would like to point out that self-referential dynamics exist in our model, and their implementation is discussed. Our mode may be applied to other developmental systems.