Seibutsu Butsuri
Online ISSN : 1347-4219
Print ISSN : 0582-4052
ISSN-L : 0582-4052
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Volume 49, Issue 3
Issue 283
Displaying 1-18 of 18 articles from this issue
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Perspective
Overview
  • Molecular Mechanisms of Gravity Perception in Higher Plants
    Moritaka NAKAMURA, Masao TASAKA, Miyo MORITA T.
    2009Volume 49Issue 3 Pages 116-121
    Published: 2009
    Released on J-STAGE: May 25, 2009
    DOIhttps://doi.org/10.2142/biophys.49.116
    JOURNAL FREE ACCESS
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    Higher plants reorient their growth direction by sensing the organ tilt relative to the direction of gravity (gravitropism). Historically famous “the starch statolith hypothesis” has explained how plants sense their organ tilt, that is, starch accumulating amyloplasts with high density sink like stones along the gravity vector in the cell, and then trigger subsequent signalings. Recent molecular genetic studies suggest that the sedimentation of amyloplasts is not a spontaneous event but is controlled by actin filaments and vacuolar membranes. This review mainly focuses on the mechanisms of gravity perception involving the amyloplasts movement and following signaling events during gravitropism.
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Review
  • Strategy of Cinnamycin and Duramycin, Peptide Toxins that Target Ethanolamine Phospholipids
    Kunihiko IWAMOTO, Asami MAKINO, Toshihide KOBAYASHI
    2009Volume 49Issue 3 Pages 122-125
    Published: 2009
    Released on J-STAGE: May 25, 2009
    DOIhttps://doi.org/10.2142/biophys.49.122
    JOURNAL FREE ACCESS
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    Cinnamycin (Ro09-0198) and duramycin are toxins of 19 amino acid cyclic peptides derived from Streptomyces species that specifically bind ethanolamine phospholipids such as phosphatidylethanolamine (PE) and phosphatidylethanolamine plasmalogen. Since PE preferentially distributes in the cytoplasmic leaflet of the plasma membrane, the strategy of the toxin seems inefficient. However, the toxins use tricks to exhibit the toxicity.
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  • Protein Minimalism: Designing on the Edge of Simplicity
    Shinya HONDA
    2009Volume 49Issue 3 Pages 126-129
    Published: 2009
    Released on J-STAGE: May 25, 2009
    DOIhttps://doi.org/10.2142/biophys.49.126
    JOURNAL FREE ACCESS
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    On the ideology of minimalism, we have designed a micro-protein consisting of only 10 amino acids. The molecule, CLN025, exhibits a β-hairpin structure in both crystalline state and aqueous solution. Thermal unfolding is shown to be reversible and can be fitted as a two-state transition. Molecular dynamics simulation starting from an extended conformation leads to a funnel-shaped surface and scale-free network, being the structures located at the bottom and the hub similar to the experimental ones. Considering these consequences, we proposed the concept of “ideal protein” as a way to clarify the differences between “protein” and “peptide”.
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Topics
Topics—Young Scientist Series
Theoretical and experimental techniques
Salon
Activity of Regional Branch
Young Voice
Letters from Abroad
Technical term
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