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2013 Fiscal Year Final Research Report

TECHNOLOGY OF NMR SIGNAL ASSIGNMENTS OF PROTEINS WITH HIGH SENSITIVITY

Research Project

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Project/Area Number 23370056
Research Category

Grant-in-Aid for Scientific Research (B)

Allocation TypeSingle-year Grants
Section一般
Research Field Structural biochemistry
Research InstitutionKitasato University

Principal Investigator

KOHNO TOSHIYUKI  北里大学, 医学部, 講師 (40416657)

Project Period (FY) 2011-04-01 – 2014-03-31
Keywords生体高分子 / NMR / タンパク質 / 安定同位体 / 微量解析 / 無細胞タンパク質合成
Research Abstract

We have improved and/or developed two methods for NMR signal assignments of large proteins with less amount of sample. At first, we improved NMR pulse programs for MAGICAL method that we previously developed with the intelligent stable isotope labeling techniques. As a result, the sensitivity of NMR measurements was dramatically enhanced by 30%. Second, we developed a new method for site-directed stable isotope labeling by changing two kinds of tRNAs of major codon and minor codon for the same amino acid. With these methods, it was indicated that NMR signals of proteins could be assigned which were difficult to analyze by using traditional NMR techniques.

  • Research Products

    (2 results)

All 2014 2013

All Journal Article (1 results) (of which Peer Reviewed: 1 results) Presentation (1 results)

  • [Journal Article] 1H, 13C and 15N backbone resonance assignments of the monomeric human M-ficolin fibrinogen-like domain secreted by Brevibacillus choshinennsis2014

    • Author(s)
      Tanio, M. Kusunoki, H. and Kohno, T
    • Journal Title

      Biomol. NMR Assign.

      Volume: 8 Pages: 207-211

    • DOI

      10.1007/s12104-013-9484-4

    • Peer Reviewed
  • [Presentation] Preparation of secretory proteins produced by Brevibacillus choshinensis for NMR study2013

    • Author(s)
      谷生道一, 楠英樹, 河野俊之
    • Organizer
      第52回NMR討論会
    • Place of Presentation
      金沢
    • Year and Date
      20131112-14

URL: 

Published: 2015-06-25  

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