Phosphorylation-Dependent Changes in Structure and Dynamics in ERK2 Detected by SDSL and EPR

Mitogen-activated protein kinases are regulated by occupancy at two phosphorylation sites near the active site cleft. Previous studies using hydrogen exchange to investigate the canonical mitogen-activated protein kinase, extracellular signal-regulated protein kinase-2, have shown that phosphorylati...

Ausführliche Beschreibung

Gespeichert in:

Bibliographische Detailangaben
Veröffentlicht in:	Biophysical journal 2004, Vol.86 (1), p.395-403
Hauptverfasser:	Hoofnagle, Andrew N., Stoner, James W., Lee, Thomas, Eaton, Sandra S., Ahn, Natalie G.
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Substitution Cysteine - chemistry Electron Spin Resonance Spectroscopy - methods Enzyme Activation Enzymes Fluid dynamics Kinetics Mitogen-Activated Protein Kinase 1 - chemistry Mitogen-Activated Protein Kinase 1 - genetics Mutagenesis, Site-Directed Phosphorylation Protein Conformation Proteins Recombinant Proteins - chemistry Spin Labels Structure-Activity Relationship
Online-Zugang:	Volltext
Tags:	Tag hinzufügen Keine Tags, Fügen Sie den ersten Tag hinzu!

Schreiben Sie den ersten Kommentar!