2-dimensional protein crystals for bioelectronics

H. Sasabe, Taiji Furuno, A. Sato, K. M. Ulmer

Research output: Chapter in Book/Report/Conference proceedingConference contribution

1 Citation (Scopus)

Abstract

A two-dimensional protein crystal that preserves biological function is necessary for the realization of bioelectronic devices. The authors have fabricated a close-packed purple membrane (PM) monolayer by the Langmuir-Blodgett technique and studied the proton transfer through the membrane under the photoexcitation. The PM monolayer is transferred to an indium-tin-oxide or Al-deposited glass substrate and/or a Si wafer by a horizontal transfer technique. The morphology of monolayer film was directly investigated by SEM. From the static and dynamic measurement of photovoltaic effect in the PM multilayer, it was confirmed that the photochemical cycle of the bacteriorhodopsin (membrane protein of PM) was preserved. The two-dimensional packing of globular protein ferritin was also investigated. Depending on the surface pressure applied, the packing changes in a chainlike aggregate or in a fairly good lattice (small patch).

Original languageEnglish
Title of host publicationIEEE/Engineering in Medicine and Biology Society Annual Conference
PublisherPubl by IEEE
Pages1003
Number of pages1
Volume10
Editionpt2
Publication statusPublished - 1988 Nov
Externally publishedYes
EventProceedings of the Annual International Conference of the IEEE Engineering in Medicine and Biology Society - New Orleans, LA, USA
Duration: 1988 Nov 41988 Nov 7

Other

OtherProceedings of the Annual International Conference of the IEEE Engineering in Medicine and Biology Society
CityNew Orleans, LA, USA
Period88/11/488/11/7

Fingerprint

Proteins
Membranes
Crystals
Monolayers
Photovoltaic effects
Proton transfer
Photoexcitation
Tin oxides
Indium
Multilayers
Glass
Scanning electron microscopy
Substrates

ASJC Scopus subject areas

  • Engineering(all)

Cite this

Sasabe, H., Furuno, T., Sato, A., & Ulmer, K. M. (1988). 2-dimensional protein crystals for bioelectronics. In IEEE/Engineering in Medicine and Biology Society Annual Conference (pt2 ed., Vol. 10, pp. 1003). Publ by IEEE.

2-dimensional protein crystals for bioelectronics. / Sasabe, H.; Furuno, Taiji; Sato, A.; Ulmer, K. M.

IEEE/Engineering in Medicine and Biology Society Annual Conference. Vol. 10 pt2. ed. Publ by IEEE, 1988. p. 1003.

Research output: Chapter in Book/Report/Conference proceedingConference contribution

Sasabe, H, Furuno, T, Sato, A & Ulmer, KM 1988, 2-dimensional protein crystals for bioelectronics. in IEEE/Engineering in Medicine and Biology Society Annual Conference. pt2 edn, vol. 10, Publ by IEEE, pp. 1003, Proceedings of the Annual International Conference of the IEEE Engineering in Medicine and Biology Society, New Orleans, LA, USA, 88/11/4.
Sasabe H, Furuno T, Sato A, Ulmer KM. 2-dimensional protein crystals for bioelectronics. In IEEE/Engineering in Medicine and Biology Society Annual Conference. pt2 ed. Vol. 10. Publ by IEEE. 1988. p. 1003
Sasabe, H. ; Furuno, Taiji ; Sato, A. ; Ulmer, K. M. / 2-dimensional protein crystals for bioelectronics. IEEE/Engineering in Medicine and Biology Society Annual Conference. Vol. 10 pt2. ed. Publ by IEEE, 1988. pp. 1003
@inproceedings{419d130712d84173828cf4430b855325,
title = "2-dimensional protein crystals for bioelectronics",
abstract = "A two-dimensional protein crystal that preserves biological function is necessary for the realization of bioelectronic devices. The authors have fabricated a close-packed purple membrane (PM) monolayer by the Langmuir-Blodgett technique and studied the proton transfer through the membrane under the photoexcitation. The PM monolayer is transferred to an indium-tin-oxide or Al-deposited glass substrate and/or a Si wafer by a horizontal transfer technique. The morphology of monolayer film was directly investigated by SEM. From the static and dynamic measurement of photovoltaic effect in the PM multilayer, it was confirmed that the photochemical cycle of the bacteriorhodopsin (membrane protein of PM) was preserved. The two-dimensional packing of globular protein ferritin was also investigated. Depending on the surface pressure applied, the packing changes in a chainlike aggregate or in a fairly good lattice (small patch).",
author = "H. Sasabe and Taiji Furuno and A. Sato and Ulmer, {K. M.}",
year = "1988",
month = "11",
language = "English",
volume = "10",
pages = "1003",
booktitle = "IEEE/Engineering in Medicine and Biology Society Annual Conference",
publisher = "Publ by IEEE",
edition = "pt2",

}

TY - GEN

T1 - 2-dimensional protein crystals for bioelectronics

AU - Sasabe, H.

AU - Furuno, Taiji

AU - Sato, A.

AU - Ulmer, K. M.

PY - 1988/11

Y1 - 1988/11

N2 - A two-dimensional protein crystal that preserves biological function is necessary for the realization of bioelectronic devices. The authors have fabricated a close-packed purple membrane (PM) monolayer by the Langmuir-Blodgett technique and studied the proton transfer through the membrane under the photoexcitation. The PM monolayer is transferred to an indium-tin-oxide or Al-deposited glass substrate and/or a Si wafer by a horizontal transfer technique. The morphology of monolayer film was directly investigated by SEM. From the static and dynamic measurement of photovoltaic effect in the PM multilayer, it was confirmed that the photochemical cycle of the bacteriorhodopsin (membrane protein of PM) was preserved. The two-dimensional packing of globular protein ferritin was also investigated. Depending on the surface pressure applied, the packing changes in a chainlike aggregate or in a fairly good lattice (small patch).

AB - A two-dimensional protein crystal that preserves biological function is necessary for the realization of bioelectronic devices. The authors have fabricated a close-packed purple membrane (PM) monolayer by the Langmuir-Blodgett technique and studied the proton transfer through the membrane under the photoexcitation. The PM monolayer is transferred to an indium-tin-oxide or Al-deposited glass substrate and/or a Si wafer by a horizontal transfer technique. The morphology of monolayer film was directly investigated by SEM. From the static and dynamic measurement of photovoltaic effect in the PM multilayer, it was confirmed that the photochemical cycle of the bacteriorhodopsin (membrane protein of PM) was preserved. The two-dimensional packing of globular protein ferritin was also investigated. Depending on the surface pressure applied, the packing changes in a chainlike aggregate or in a fairly good lattice (small patch).

UR - http://www.scopus.com/inward/record.url?scp=0024111008&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0024111008&partnerID=8YFLogxK

M3 - Conference contribution

AN - SCOPUS:0024111008

VL - 10

SP - 1003

BT - IEEE/Engineering in Medicine and Biology Society Annual Conference

PB - Publ by IEEE

ER -