Monitoring of Actin Unfolding by Room Temperature Tryptophan Phosphorescence

Slow intramolecular mobility of native and inactivated actin from rabbit skeletal muscle during the process of protein unfolding induced by GdnHCl was studied using tryptophan room temperature phosphorescence (RTP). By this method, the conclusion was confirmed that an essentially unfolded intermedia...

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Veröffentlicht in:	Biochemistry (Easton) 2003-11, Vol.42 (46), p.13551-13557
Hauptverfasser:	Mazhul', Vladimir M, Zaitseva, Ekaterina M, Shavlovsky, Mikhail M, Stepanenko, Olesia V, Kuznetsova, Irina M, Turoverov, Konstantin K
Format:	Artikel
Sprache:	eng
Schlagworte:	Actins - chemistry Animals Guanidine - chemistry Kinetics Luminescent Measurements Muscle, Skeletal - chemistry Protein Denaturation Protein Folding Rabbits Temperature Tryptophan - chemistry
Online-Zugang:	Volltext
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