Protein Nucleation Triggered by Femtosecond Laser-Induced Cavitation Bubbles(<Special Issue>Light-induced Crystal Growth)

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  • Yoshikawa Hiroshi
    Department of Chemistry, Saitama University:Graduate School of Engineering, Osaka University
  • Murai Ryota
    Graduate School of Engineering, Osaka University:Graduate School of Energy Science, Kyoto University
  • Sugiyama Shigeru
    Graduate School of Engineering, Osaka University
  • Adachi Hiroaki
    Graduate School of Engineering, Osaka University:SOSHO Inc.
  • Matsumura Hiroyoshi
    Graduate School of Engineering, Osaka University:SOSHO Inc.
  • Inoue Tsuyoshi
    Graduate School of Engineering, Osaka University:SOSHO Inc.
  • Murakami Satoshi
    SOSHO Inc.:Graduate School of Bioscience and Biotechnology, Tokyo Institute of Technology
  • Takano Kazufumi
    SOSHO Inc.:Graduate School of Life and Environmental Sciences. Kyoto Prefectural University
  • Mori Yusuke
    Graduate School of Engineering, Osaka University:SOSHO Inc.

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Other Title
  • フェムト秒レーザー誘起キャビテーションバブルによるタンパク質の結晶核発生(<特集>光で成長する結晶)
  • フェムト秒レーザー誘起キャビテーションバブルによるタンパク質の結晶核発生
  • フェムトビョウ レーザー ユウキ キャビテーションバブル ニ ヨル タンパクシツ ノ ケッショウカク ハッセイ

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Abstract

Focused irradiation of femtosecond laser pulses can induce nucleation of various proteins at low supersaturation, where high quality protein crystals can be obtained. Recently we studied the nucleation mechanism by fast-imaging methods and found that the rapid shrinkage (microsecond-scale) of a laser-induced cavitation bubble creates a local high concentration of protein. Actually, the surface of cavitation bubbles is known to be a preferred region for protein adsorption. Hence, protein molecules adsorbed at the surface during the expansion will be then gathered to the center region by the rapid shrinking of cavitation bubbles. These results indicate the femtosecond laser technique is based on a fundamental crystallization parameter, concentration, and can work as a nucleation trigger of various materials. In this paper, we introduce our recent studies of the nucleation mechanism and the development of the technique for protein nucleation at lower supersaturation.

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