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

抄録

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.