Nanosecond Dynamics of Tryptophans in Different Conformational States of Apomyoglobin Proteins

Fluorescence anisotropy kinetics were employed to quantify the nanosecond mobility of tryptophan residues in different conformational states (native, molten globule, unfolded) of apomyoglobins. Of particular interest is the similarity between the fluorescence anisotropy decays of tryptophans in the...

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Veröffentlicht in:	Biochemistry (Easton) 2000-02, Vol.39 (7), p.1879-1889
Hauptverfasser:	Tcherkasskaya, Olga, Ptitsyn, Oleg B, Knutson, Jay R
Format:	Artikel
Sprache:	eng
Schlagworte:	Animals Apoproteins - chemistry Diffusion Fluorescence Polarization - methods Horses Kinetics Myoglobin - chemistry Protein Conformation Protein Folding Spectrometry, Fluorescence Thermodynamics Time Factors Tryptophan - chemistry Tuna Whales
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