Seibutsu Butsuri
Online ISSN : 1347-4219
Print ISSN : 0582-4052
ISSN-L : 0582-4052
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Volume 45, Issue 1
Issue 257
Displaying 1-14 of 14 articles from this issue
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Perspective
Overview
  • Hydration and Solute Binding of Protein: Relation to Preferential Interaction
    Tsutomu ARAKAWA, Yoshiko KITA
    2005 Volume 45 Issue 1 Pages 4-9
    Published: 2005
    Released on J-STAGE: January 25, 2005
    DOIhttps://doi.org/10.2142/biophys.45.4
    JOURNAL FREE ACCESS
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    Solutes at high concentration, e.g., above 0.1-0.5 M, are often required during purification, storage and analysis of proteins. The fact that high concentrations are required implies that the interactions of the solutes with the proteins are weak, yet play a major role in these processes of the proteins. Interactions that occur at such high concentrations are called “preferential interactions” and are related to hydration and solute binding of the proteins. This short chapter describes the relation between preferential interaction and binding of water and solutes with the proteins.
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  • Progress in a Study of Ion Channels for 50 Years
    Fumio KUKITA
    2005 Volume 45 Issue 1 Pages 10-15
    Published: 2005
    Released on J-STAGE: January 25, 2005
    DOIhttps://doi.org/10.2142/biophys.45.10
    JOURNAL FREE ACCESS
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    Modern neurophysiology based on ion channels was born a half century ago by Hodgkin and Huxley’s memorial works on ionic currents in squid giant axon. Their finding leads to identification of ion channel proteins containing a voltage-sensor and an aqueous pore. Patch clamping and molecular biological techniques have accelerated to understand how ion channels work. Quite recently we have started to understand ion channel functions on the basis of 3D-structure. This review overviewed a half century progress in understanding of ion channels.
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Review
  • Changes in Cytoplasmic Domain Organization and Energy Transduction in Calcium Pump
    Hiroshi SUZUKI
    2005 Volume 45 Issue 1 Pages 16-21
    Published: 2005
    Released on J-STAGE: January 25, 2005
    DOIhttps://doi.org/10.2142/biophys.45.16
    JOURNAL FREE ACCESS
    Supplementary material
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    Sarco(endo)plasmic reticulum Ca2+-ATPase catalyzes Ca2+ transport coupled with ATP hydrolysis. It will be reviewed here to understand mechanism of energy transduction in the transport that how large motions of 3 cytoplasmic domains occur during the isomeric transition of phosphorylated intermediates and how these changes can be transmitted to the transport sites in transmembrane domain to release the bound Ca2+ into lumen. Stable analogs for the phosphorylated intermediates were developed for structural studies and their biochemical characterization to reveal the coupled changes in the catalytic and transport sites is also described.
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  • The Mechanism of the Ion-Driven Flagellar Motor Rotation: Where Is the Rotational Force Generated?
    Hajime FUKUOKA, Toshiharu YAKUSHI, Michio HOMMA
    2005 Volume 45 Issue 1 Pages 22-27
    Published: 2005
    Released on J-STAGE: January 25, 2005
    DOIhttps://doi.org/10.2142/biophys.45.22
    JOURNAL FREE ACCESS
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    Bacterial flagellar motors are molecular machines powered by the electrochemical potential gradient of specific ions, H+ or Na+, across the membrane. The force is generated by the interaction between a stator and a rotor of the motor which is located at the base of flagellum. A mechanical model of the H+-driven motor rotation by electrostatic interactions between the stator protein, MotA, and the rotor protein, FliG, has been presented. In this review, we summarize recent studies of the Na+-driven motor and discuss the molecular mechanism of the rotation comparing with the H+-driven motor.
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Topics
Theoretical and experimental techniques
Salon
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