Dynamics of parvalbumin studied by fluorescence emission and triplet absorption spectroscopy of tryptophan
Fluorescence emission and triplet-triplet absorbance spectroscopy of the single tryptophan in cod parvalbumin were used to study the stability and dynamics of the protein as influenced by Ca2+ binding and interaction with a chaotropic agent. The concentrations for half-saturation for Ca binding were...
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Veröffentlicht in: | Biochemistry (Easton) 1995, Vol.34 (4), p.1355-1363 |
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