Proximity relationships of tryptophanyl residues and oxygen binding site in Levantina hierosolima hemocyanin. A fluorimetric study
- 17 October 1978
- journal article
- research article
- Published by American Chemical Society (ACS) in Biochemistry
- Vol. 17 (21) , 4438-4442
- https://doi.org/10.1021/bi00614a013
Abstract
No abstract availableThis publication has 16 references indexed in Scilit:
- A resonance Raman study of the copper protein, hemocyanin. New evidence for the structure of the oxygen-binding siteJournal of the American Chemical Society, 1976
- Homogeneity and variability in the structure of azurin molecules studied by fluorescence decay and circular polarizationBiochemistry, 1975
- An improvement of nanosecond fluorimeters to overcome drift problemsReview of Scientific Instruments, 1974
- Acid-base titration of hemocyanin from Octopus vulgarisBiochemistry, 1974
- FLUORESCENCE AND THE LOCATION OF TRYPTOPHAN RESIDUES IN PROTEIN MOLECULESPhotochemistry and Photobiology, 1973
- Structure of the carbon monoxide binding site of hemocyanins studied by Fourier transform infrared spectroscopyBiochemistry, 1972
- Fluorescence properties of hemocyanin from Levantina hierosolimaBiochemistry, 1970
- The Croonian Lecture, 1968 - The haemoglobin moleculeProceedings of the Royal Society of London. B. Biological Sciences, 1969
- The selective quenching of tryptophan fluorescence in proteins by iodide ion: Lysozyme in the presence and absence of substrateBiochemical and Biophysical Research Communications, 1967
- Fluorescence Polarization: Measurement with Ultraviolet-Polarizing Filters in a SpectrophotofluorometerScience, 1965