Structural Study of the N-Terminal Domain of the Alpha Subunit of Escherichia coli RNA Polymerase Solubilized with Non-Denaturing Detergents

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概要

• 論文の詳細を見る
• Japanese Biochemical Societyの論文
• 2000-08-01

著者

• KYOGOKU Yoshimasa

  Institute for Protein Research, Osaka University

• Kyogoku Y

  Osaka Univ. Osaka

• Kyogoku Yoshimasa

  Institute For Protein Research Osaka University

• OTOMO Takanori

  Institute for Protein Research, Osaka University

• YAMAZAKI Toshio

  Institute for Protein Research, Osaka University

• MURAKAMI Katsuhiko

  National Institute of Genetics

• ISHIHARA Akira

  National Institute of Genetics

• Otomo Takanori

  Institute For Protein Research Osaka University

• Yamazaki Toshio

  Institute For Protein Research Osaka University

• Murakami K

  Nkk Techno‐service Co. Kawasaki Jpn

関連論文

• Nuclear Magnetic Resonance Study of Complexes between CRP and Its 22-and 28-Base-Pair Operators^1
• Structural Study of the N-Terminal Domain of the Alpha Subunit of Escherichia coli RNA Polymerase Solubilized with Non-Denaturing Detergents
• Resonance Assignments, Solution Structure, and Backbone Dynamics of the DNA- and RPA-Binding Domain of Human Repair Factor XPA
• Cloning of the RNA polymerase α Subunit Gene from Thermus thermophilus HB8 and Characterization of the Protein
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• Solution Structure of ACTH(1-24) by Means of Multinuclear and Multidimensional NMR Spectroscopy
• Characterization and Comparison of Synthetic Immobile and Mobile Holliday Junctions
• Detection of the Protein-Protein Interaction between Cyclic AMP Receptor Protein and RNA Polymerase, by ^C-Carbonyl NMR^1
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• 13C-NMR study of aerosol OT in chloroform.
• Correlation NMR spectroscopy with a water signal subtracting system.
• Detection of the Protein-Protein Interaction between Cyclic AMP Receptor Protein and RNA Polymerase, by 13C-Carbonyl NMR.

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