New developments in structural analysis of protens by synchrotron-radiation vacuum-ultraviolet circular dichroism

2014 Fiscal Year Final Research Report

• Project/Area Number: 23687020
• Research Category: Grant-in-Aid for Young Scientists (A)
• Allocation Type: Single-year Grants
• Research Field: Biophysics
• Research Institution: Hiroshima University
• Principal Investigator: MATSUO Koichi 広島大学, 放射光科学研究センター, 助教 (40403620)
• Project Period (FY): 2011-04-01 – 2015-03-31
• Keywords: 真空紫外円二色性 / 放射光 / 蛋白質 / 二次構造 / バイオインフォマティクス / 円二色性理論 / 生体膜 / アミロイド

Outline of Final Research Achievements

We newly developed the analytical method for estimating the contents, numbers of segments, sequences, and orientations of protein secondary structures in aqueous solution using a vacuum-ultraviolet circular dichroism (VUVCD) with a synchrotron-radiation light source. This spectroscopy was powerful technique for characterizing the structures of proteins at non-native states such as the membrane-bound state. The VUVCD spectrum of amyloid fibrils was assigned with the CD theory and molecular dynamics simulation to characterize the intermolecular structures of amyloid fibrils which are important for understanding the fibril formations and toxicity. A press release of this research was issued to the media. Further, we invited 14 domestic and international experts of CD fields and organized Hiroshima International Workshop on Circular Dichroism (4th May, 2014, Hiroshima) to promote the usage of protein structural analysis using the VUVCD spectroscopy.

Free Research Field

生物物理化学