Two-dimensional arrangement of a functional protein by cysteine-gold interaction: Enzyme activity and characterization of a protein monolayer on a gold substrate

Yuji C. Sasaki, Kenji Yasuda, Yoshio Suzuki, Tadashi Ishibashi, Isamu Satoh, Yasutake Fujiki, Shin'ichi Ishiwata

研究成果: Article査読

53 被引用数 (Scopus)

抄録

We have characterized the functional protein, myosin subfragment 1 (S1), attached to a gold substrate by the sulfhydryl groups of cysteine in proteins. The amino groups of the regulatory light chain (RLC) isolated from myosin were labeled with a radioisotope (125I), and the labeled RLC was incorporated into S1 from which the RLC had been removed. The radiation from 125I showed that S1 molecules had attached to the gold and, through the interference effect of the monochromatic radiation from 125I, provided information about the position of labeled RLC sites in the S1 monolayer. The interference fringes showed that the RLC was located close to the gold surface and that all of the adsorbed S1 molecules had the same orientation. We confirmed that the motor function of S1 on the gold surface is maintained by observing sliding movement at low ionic strength and by observing the detachment at high ionic strength of fluorescent actin filaments in the presence of ATP. We also found that the adsorbed S1 molecules were not removed from the Au surface by a reducing agent. Thus the Au-S bond is more stable than the S-S bond.

本文言語English
ページ(範囲)1842-1848
ページ数7
ジャーナルBiophysical Journal
72
4
DOI
出版ステータスPublished - 1997 4
外部発表はい

ASJC Scopus subject areas

  • 生物理学

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