Phosphorescence studies of the interaction of myelin basic protein with phosphatidylserine vesicles

Phosphorescence from the lone tryptophan residue has been studied to monitor the interaction of myelin basic protein with phosphatidylserine vesicles. Spectral shifts in the phosphorescence of the protein in a glycerol-buffer (70:30 w/w) solvent at low temperature are consistent with fluorescence da...

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Veröffentlicht in:	Biochemistry (Easton) 1981-05, Vol.20 (11), p.3110-3116
Hauptverfasser:	Vadas, Elizabeth B, Melancon, Paul, Braun, Peter E, Galley, William C
Format:	Artikel
Sprache:	eng
Schlagworte:	Animals Brain Kinetics Luminescent Measurements Myelin Basic Protein Phosphatidylserines Protein Binding Protein Conformation Rats Spectrometry, Fluorescence Tryptophan - analysis Tyrosine - analysis
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