Molecular Mechanisms of Membrane Proteins Studied by Infrared Spectroscopy

• Furutani Yuji

  Institute for Molecular Science The Graduate University for Advanced Studies [SOKENDAI] JST PRESTO “Chemical conversion of light energy”

Bibliographic Information

Other Title

• 赤外分光法による膜タンパク質の分子機構研究

Abstract

Membrane proteins are indispensable for cell signaling, bioenergetics, and transportation. Atomic structures of membrane proteins have been elucidated by methods in structural biology (e.g. X-ray crystallography). Structural changes of them in action should be investigated to improve the understanding of the molecular mechanisms in more detail. Infrared spectroscopy is a powerful method to analyze structural changes of protein by combining it with various kinds of stimulus-induced difference spectroscopic techniques. In this review article, my recent studies on microbial rhodopsin, ion channel and ion pump proteins are summarized. Light-induced difference infrared spectroscopy revealed the hydrogen-bonding change of Thr204 in pharaonis phoborhodopsin upon photoisomerization of the retinal chromophore, which turned out to be a key residue for the signal transduction. Attenuated total reflection (ATR) method was applied on the studies of ion-protein interaction of a potassium channel, KcsA, and a sodium pump, V-type ATPase. Finally, development of a rapid-buffer exchange apparatus for time-resolved ATR infrared spectroscopy is introduced, which would be a powerful technique for investigating ion- and ligand-binding reactions of membrane proteins.

Journal

• Molecular Science

  Molecular Science 8 (1), A0067-, 2014

  Japan Society for Molecular Science

Keywords

• rhodopsin
• ion channel
• ion pump
• transporter
• FT-IR

Details

• CRID: 1390001205282052992
• NII Article ID: 130004688035
• DOI: 10.3175/molsci.8.a0067
• ISSN: 18818404
• Text Lang: ja
• Data Source:
  • JaLC
  • Crossref
  • CiNii Articles
  • KAKEN
• Abstract License Flag: Disallowed