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Volumn 40, Issue 49, 2001, Pages 14952-14959

FTIR studies of phytochrome photoreactions reveal the C=O bands of the chromophore: Consequences for its protonation states, conformation, and protein interaction

(6) Foerstendorf, H a Benda, C b Gartner W b,c Storf, M d Scheer, H d Siebert, F a

a UNIVERSITY OF FREIBURG (Germany)

b MAX PLANCK INSTITUTE OF BIOCHEMISTRY (Germany)

c MAX PLANCK INSTITUTE FOR CHEMICAL ENERGY CONVERSION (Germany)

d UNIVERSITY OF MUNICH (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

PHOTOPRODUCTS;

CHEMICAL MODIFICATION; CHROMOPHORES; FOURIER TRANSFORM INFRARED SPECTROSCOPY; PHOTOCHEMICAL REACTIONS;

PROTEINS;

PHYTOCHROME; RECOMBINANT PROTEIN;

ARTICLE; FOURIER TRANSFORMATION; INFRARED SPECTROSCOPY; MOLECULAR DYNAMICS; NONHUMAN; PHOTOCHEMISTRY; PHOTORECEPTOR; PHYTOCHEMISTRY; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN DOMAIN; PROTEIN PROTEIN INTERACTION; PROTEIN STABILITY; PROTON TRANSPORT;

AVENA SATIVA; MOLECULAR STRUCTURE; OXYGEN RADIOISOTOPES; PEPTIDE FRAGMENTS; PHYTOCHROME; PROTEIN CONFORMATION; RECOMBINANT PROTEINS; SPECTROSCOPY, FOURIER TRANSFORM INFRARED;

EID: 0035846628 PISSN: 00062960 EISSN: None Source Type: Journal
DOI: 10.1021/bi0156916 Document Type: Article

Times cited : (81)

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