Two-dimensional molecular packing of proteins

H. Sasabe, T. Furuno, J. Otomo, H. Tomioka, Y. Urabe, T. Nagamune, K. H. Kim, K. Kobayashi, Y. Kobayashi

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Abstract

A technique involving the physical and/or chemical adsorption of molecules in the subphase to the interfacial Langmuir monolayer has been developed to arrange protein molecules such as ferritin, bacteriorhodopsin (BR) (purple membrane) and cytochrome b562 in closely-packed two dimensional arrays. For better packing of molecules, site-directed mutagenesis of cytochrome b562 was introduced to enhance the hydrophobicity or to stabilize the molecules by introducing a cystine linkage. The photoreaction cycle of BR was analysed. From the sequence analysis of newly isolated BR-like pigments, it was suggested that several amino acid residues around the retinal were conserved and formed a "retinal pocket".

Original languageEnglish
Pages (from-to)99-104
Number of pages6
JournalThin Solid Films
Volume216
Issue number1
DOIs
Publication statusPublished - 1992 Aug 28

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ASJC Scopus subject areas

  • Electronic, Optical and Magnetic Materials
  • Surfaces and Interfaces
  • Surfaces, Coatings and Films
  • Metals and Alloys
  • Materials Chemistry

Cite this

Sasabe, H., Furuno, T., Otomo, J., Tomioka, H., Urabe, Y., Nagamune, T., Kim, K. H., Kobayashi, K., & Kobayashi, Y. (1992). Two-dimensional molecular packing of proteins. Thin Solid Films, 216(1), 99-104. https://doi.org/10.1016/0040-6090(92)90877-E