Seibutsu Butsuri
Online ISSN : 1347-4219
Print ISSN : 0582-4052
ISSN-L : 0582-4052
Search
Advanced search
OR
Browse
Search
Volume 44, Issue 5
Issue 255
Displaying 1-13 of 13 articles from this issue
Show all abstracts
    • |<
    • <
    • 1
    • >
    • >|
Perspective
Overview
Review
  • The Genes Encoding Redox Proteins from Sulfate-Reducing Bacteria and their Structures
    Masaya KITAMURA, Yoshiki HIGUCHI
    2004 Volume 44 Issue 5 Pages 206-211
    Published: 2004
    Released on J-STAGE: September 28, 2004
    DOIhttps://doi.org/10.2142/biophys.44.206
    JOURNAL FREE ACCESS
    Supplementary material
    Show abstractHide abstract
    Sulfate-reducing bacteria, one of the anaerobic prokaryotes, have many redox proteins. They use dissimilatory sulfate reduction, but there still remain many uncovered questions about this system. Here we describe the recent progress in genetical and structural studies about these proteins, especially, cytochrome c3, high-molecular-weight cytochrome c, hydrogenase, flavoproteins, and the defense proteins against oxygen toxicity with genomic information of D. vulgaris.
    View full abstract
    Download PDF (310K)
  • Structure and Formation of Amyloid Fibrils of β2-Microglobulin
    Kei-ichi YAMAGUCHI, Yuji GOTO
    2004 Volume 44 Issue 5 Pages 212-217
    Published: 2004
    Released on J-STAGE: September 28, 2004
    DOIhttps://doi.org/10.2142/biophys.44.212
    JOURNAL FREE ACCESS
    Show abstractHide abstract
    Amyloid fibril formation is a phenomenon common to many proteins and peptides. Clarifying the mechanism of amyloid fibril formation is essential not only for understanding the pathogenesis of amyloidosis but also for improving our understanding of the mechanism of protein folding. Dialysis-related amyloidosis is a common and serious complication among patients on long-term hemodialysis, in which β2-microglobulin forms amyloid fibrils. We studied the core of fibrils at single-residue resolution using recently developed H/D exchange method with the dissolution of fibrils by dimethylsulfoxide. The results suggest the mechanism of amyloid fibril formation, in which the core β-sheet formed by a minimal sequence propagates to form a rigid and extensive β-sheet network.
    View full abstract
    Download PDF (499K)
Topics
Experimental techniques
Salon
Technical term
    • |<
    • <
    • 1
    • >
    • >|
feedback
 Top