Biopolymer. High Pressure NMR Enabling a Wide Conformational Search of Proteins.

• AKASAKA Kazuyuki

  Department of Molecular Science, Graduate School of Science and Technology, Kobe University

Bibliographic Information

Other Title

• 生体高分子　　高圧ＮＭＲによる蛋白質研究の新しい展開　　広い構造アンサンブルの探索
• コウアツ NMR ニ ヨル タンパクシツ ケンキュウ ノ アタラシイ テンカイ ヒロイ コウゾウ アンサンブル ノ タンサク
• 広い構造アンサンブルの探索

Abstract

Many proteins are considered to perform their functions by dynamic excursion to “other” conformations that deviate from the basic structure found in crystal. These “other” conformations have seldom become targets of detailed structural study. The on-line cell high pressure NMR technique developed at Kobe is the only available technique capable of producing “other” conformations of proteins and simultaneously reporting their structures at residue-specific resolution using multi-dimensional NMR spectroscopy. The principle is based on the recognition that the partial molar volume of a protein strongly depends on its conformational state. Examples are given from two proteins, basic pancreatic trypsin inhibitor and the Ras-binding domain of RalGEF.

Journal

• The Review of High Pressure Science and Technology

  The Review of High Pressure Science and Technology 10 (2), 88-94, 2000

  The Japan Society of High Pressure Science and Technology

Keywords

• high pressure NMR
• partial molar volume
• protein conformation
• pressure denaturation
• local unfolding
• multi-dimensional NMR
• structural fluctuation
• conformational ensemble

Details

• CRID: 1390001204381135360
• NII Article ID: 10004668570
• NII Book ID: AN10452913
• DOI: 10.4131/jshpreview.10.88
• COI: 1:CAS:528:DC%2BD3cXltFyrtbo%3D
• ISSN: 13481940
• ISSN: 0917639X
• ISSN: http://id.crossref.org/issn/0917639X
• NDL BIB ID: 5358044
• Web Site: https://ndlsearch.ndl.go.jp/books/R000000004-I5358044
• Text Lang: ja
• Data Source:
  • JaLC
  • NDL
  • Crossref
  • CiNii Articles
• Abstract License Flag: Disallowed