Thermally induced structural changes of intrinsically disordered small heat shock protein Hsp22

We applied different methods (differential scanning calorimetry, circular dichroism, Fourier transform infrared spectroscopy, and intrinsic fluorescence) to investigate the thermal-induced changes in the structure of small heat shock protein Hsp22. It has been shown that this protein undergoes therm...

Ausführliche Beschreibung

Gespeichert in:

Bibliographische Detailangaben
Veröffentlicht in:	Biophysical chemistry 2009-12, Vol.145 (2), p.79-85
Hauptverfasser:	Kazakov, Alexey S., Markov, Denis I., Gusev, Nikolai B., Levitsky, Dmitrii I.
Format:	Artikel
Sprache:	eng
Schlagworte:	Actins - metabolism alpha-Crystallins - chemistry Calorimetry, Differential Scanning Differential scanning calorimetry Downhill folding Heat-Shock Proteins - chemistry Heat-Shock Proteins - genetics Heat-Shock Proteins - metabolism Heat-Shock Proteins - pharmacology Hot Temperature Humans Intrinsically disordered proteins Mutation Protein Binding - drug effects Protein Denaturation Protein Folding Protein Structure, Secondary Protein Structure, Tertiary Protein-Serine-Threonine Kinases - chemistry Protein-Serine-Threonine Kinases - genetics Protein-Serine-Threonine Kinases - metabolism Protein-Serine-Threonine Kinases - pharmacology Small heat shock proteins Thermal unfolding Tryptophan fluorescence
Online-Zugang:	Volltext
Tags:	Tag hinzufügen Keine Tags, Fügen Sie den ersten Tag hinzu!

Schreiben Sie den ersten Kommentar!