Internal Dynamics of Lactose Permease

The transport protein lactose permease was reconstituted in vesicles of dimyristoylphosphatidylcholine, and the internal dynamics were studied by measuring the fluorescence anisotropy decay of the tryptophan residues and of a covalently bound pyrene label. For the tryptophans three relaxation proces...

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Veröffentlicht in:	Proceedings of the National Academy of Sciences - PNAS 1989-12, Vol.86 (24), p.9827-9831
Hauptverfasser:	Dornmair, Klaus, Jähnig, Fritz
Format:	Artikel
Sprache:	eng
Schlagworte:	Anisotropy Biological and medical sciences Cell Membrane - enzymology Conformational dynamics in molecular biology Dimyristoylphosphatidylcholine Ellipsoids Escherichia coli - enzymology Escherichia coli Proteins Fluorescence Fluorescence Polarization Fluorescent Dyes Fundamental and applied biological sciences. Psychology Lipids Liposomes Maleimides Membrane proteins Membrane transport proteins Membrane Transport Proteins - metabolism membrane vesicles Molecular biophysics Monosaccharide Transport Proteins Protein Conformation Relaxation time Rotation Symporters Temperature dependence Thermodynamics Time windows Tryptophan
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