核磁気共鳴法を用いた細胞内タンパク質の無侵襲解析

DOI Web Site Web Site PubMed 参考文献25件 オープンアクセス

書誌事項

タイトル別名
  • Non-invasive Analysis of Proteins in Living Cells Using NMR Spectroscopy
  • Symposium Review 核磁気共鳴法を用いた細胞内タンパク質の無侵襲解析
  • Symposium Review カク ジキ キョウメイホウ オ モチイタ サイボウ ナイ タンパクシツ ノ ムシンシュウカイセキ

この論文をさがす

抄録

  NMR spectroscopy enables structural analyses of proteins and has been widely used in the structural biology field in recent decades. NMR spectroscopy can be applied to proteins inside living cells, allowing characterization of their structures and dynamics in intracellular environments. The simplest “in-cell NMR” approach employs bacterial cells; in this approach, live Escherichia coli cells overexpressing a specific protein are subjected to NMR. The cells are grown in an NMR active isotope-enriched medium to ensure that the overexpressed proteins are labeled with the stable isotopes. Thus the obtained NMR spectra, which are derived from labeled proteins, contain atomic-level information about the structure and dynamics of the proteins. Recent progress enables us to work with higher eukaryotic cells such as HeLa and HEK293 cells, for which a number of techniques have been developed to achieve isotope labeling of the specific target protein. In this review, we describe successful use of electroporation for in-cell NMR. In addition, 19F-NMR to characterize protein-ligand interactions in cells is presented. Because 19F nuclei rarely exist in natural cells, when 19F-labeled proteins are delivered into cells and 19F-NMR signals are observed, one can safely ascertain that these signals originate from the delivered proteins and not other molecules.<br>

収録刊行物

  • 薬学雑誌

    薬学雑誌 135 (3), 391-398, 2015-03-01

    公益社団法人 日本薬学会

参考文献 (25)*注記

もっと見る

関連プロジェクト

もっと見る

キーワード

詳細情報 詳細情報について

問題の指摘

ページトップへ