Variable Pressure NMR Study of Protein Dynamics

DOI

Bibliographic Information

Other Title
  • 可変圧力ＮＭＲ法による蛋白質の準安定構造解析

Abstract

Pressure shifts the equilibrium distribution of conformers of a protein through volume differences. Here, we examined the dynamics of ubiquitin and ubiquitin-like proteins by utilizing variable pressure NMR spectroscopy. Ubiquitin is a highly conserved 76 amino acid residue protein, whose sequence is extremely well conserved in all eukaryote. The same topology of folding frequently occurs in proteins, which are named ubiquitin-like proteins (ubl), despite the fact that the sequence identity among the ubl is rather poor. Further investigation of common structural motifs in a wider conformational state may provide additional information why proteins conserve similar topology. Thus by using variable pressure NMR techniques, we explored structures of ubiqitin and the two ubl, NEDD8, and SUMO-2, in a wide conformational space, namely in their energy landscape. We found similar conformational fluctuations among the ubl in the evolutionary conserved enzyme-binding region of the ubl, namely ubiquitin, NEDD8 and SUMO-2, indicating a conserved structural and thermodynamic design for their function.

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Details 詳細情報について

  • CRID
    1390282680263135744
  • NII Article ID
    130004503894
  • DOI
    10.11229/hpbb.2.8
  • ISSN
    18821723
  • Text Lang
    ja
  • Data Source
    • JaLC
    • CiNii Articles
  • Abstract License Flag
    Disallowed

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