Circular dichroism of phytochrome intermediates-Reference-Cited by-同舟云学术

Circular dichroism of phytochrome intermediates

Published:1988-09 Issue:1 Volume:74 Page:169-175
ISSN:0031-9317
Container-title:Physiologia Plantarum
language:en
Short-container-title:Physiol Plant

Author:

Eilfeld Petra H.,Eilfeld Peter G.

Publisher

Wiley

Subject

Cell Biology,Plant Science,Genetics,General Medicine,Physiology

Link

http://onlinelibrary.wiley.com/wol1/doi/10.1111/j.1399-3054.1988.tb04959.x/fullpdf

Reference28 articles.

1. Laser flash photolysis of 124-kilodalton oat phytochrome in water and deuterium oxide solutions: formation and decay of the I700 intermediates

2. Low-temperature absorption and circular dichroism studies of phytochrome

3. C. R. Cantor, and P. R. Schimmel, 1980 . Biophysical chemistry. Part II. Techniques for the study of biophysical structure and function . - W. H. Freeman and Co., San Francisco. pp.409 -432 . ISBN 0-7167-1190-7.

4. A photoreversible circular dichroism spectral change in oat phytochrome is suppressed by a monoclonal antibody that binds near its N-terminus and by chromophore modification

5. LOW-TEMPERATURE STUDIES ON PHYTOCHROME: LIGHT AND DARK REACTIONS IN THE RED TO FAR-RED TRANSFORMATION AND NEW INTERMEDIATE FORMS OF PHYTOCHROME

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1. Optical activity and stereochemistry of linear oligopyrroles and bile pigments;Tetrahedron: Asymmetry;1999-02

2. Phytochromes: molecular structure, photoreceptor process and physiological function;Concepts in Photobiology;1999

3. Photobiophysics and photobiochemistry of the heterogeneous phytochrome system;Biochimica et Biophysica Acta (BBA) - Bioenergetics;1995-03

4. ULTRAVIOLET RESONANCE RAMAN SPECTRA OF PHYTOCHROME: A COMPARISON OF THE ENVIRONMENTS OF TRYPTOPHAN SIDE CHAINS BETWEEN RED LIGHT-ABSORBING AND FAR-RED LIGHT-ABSORBING FORMS;Photochemistry and Photobiology;1993-02

5. [7] Nanosecond time-resolved absorption and polarization dichroism spectroscopies;Metallobiochemistry Part C: Spectroscopic and Physical Methods for Probing Metal Ion Environments in Metalloenzymes and Metalloproteins;1993