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Toward oxygen binding curves of single respiratory proteins

Title data

Erker, Wolfgang ; Lippitz, Markus ; Basche, Thomas ; Decker, Heinz:
Toward oxygen binding curves of single respiratory proteins.
In: Micron. Vol. 35 (2004) Issue 1-2 . - pp. 111-113.
ISSN 1878-4291
DOI: https://doi.org/10.1016/j.micron.2003.10.037

Abstract in another language

Oxygen binding curves of single molecules promise to discriminate between different models describing cooperativity because load distributions are accessible. Individual tarantula hemocyanins could be detected by fluorescence correlation spectroscopy using intrinsic tryptophan fluorescence as sensor of bound oxygen. However, imaging of immobilized proteins was not possible due to fast photo-bleaching. It is shown that tetra-methyl-carboxy-rhodamine (TAMRA), commonly used as a fluorescence label in single-molecule spectroscopy, can also be applied to monitor bound oxygen. The dye's fluorescence is quenched due to Forster energy transfer to the oxygenated active sites of hemocyanin. (C) 2003 Elsevier Ltd. All rights reserved.

Further data

Item Type: Article in a journal
Refereed: Yes
Institutions of the University: Faculties > Faculty of Mathematics, Physics und Computer Science > Department of Physics > Lehrstuhl Experimentalphysik III - Nanooptik
Faculties > Faculty of Mathematics, Physics und Computer Science > Department of Physics > Lehrstuhl Experimentalphysik III - Nanooptik > Lehrstuhl Experimentalphysik III - Nanooptik - Univ.-Prof. Dr. Markus Lippitz
Faculties
Faculties > Faculty of Mathematics, Physics und Computer Science
Faculties > Faculty of Mathematics, Physics und Computer Science > Department of Physics
Result of work at the UBT: No
DDC Subjects: 500 Science > 530 Physics
Date Deposited: 17 Dec 2015 08:10
Last Modified: 17 Dec 2015 08:10
URI: https://eref.uni-bayreuth.de/id/eprint/28974