Double Histidine Based EPR Measurements at Physiological Temperatures Permit Site‐Specific Elucidation of Hidden Dynamics in Enzymes

Protein dynamics is at the heart of all cellular processes. Here, we utilize the dHis‐CuIINTA label to obtain site‐specific information on dynamics for both an α‐helix and β‐sheet site of GB1, the immunoglobulin binding domain of protein G. Spectral features found in our CW‐EPR measurements were con...

Ausführliche Beschreibung

Gespeichert in:

Bibliographische Detailangaben
Veröffentlicht in:	Angewandte Chemie International Edition 2020-12, Vol.59 (51), p.23040-23044
Hauptverfasser:	Singewald, Kevin, Bogetti, Xiaowei, Sinha, Kaustubh, Rule, Gordon S, Saxena, Sunil
Format:	Artikel
Sprache:	eng
Schlagworte:	Binding continuous wave Coordination Complexes - chemistry Coordination Complexes - metabolism copper Copper - chemistry Copper - metabolism Electron Spin Resonance Spectroscopy EPR spectroscopy Glutathione Glutathione transferase Glutathione Transferase - chemistry Glutathione Transferase - metabolism Histidine Histidine - chemistry Histidine - metabolism Humans Isoenzymes - chemistry Isoenzymes - metabolism Labeling Molecular Conformation Molecular dynamics Molecular Dynamics Simulation Nitrilotriacetic Acid - chemistry Nitrilotriacetic Acid - metabolism protein dynamics Protein G Proteins Room temperature spin labelling Substrates Temperature
Online-Zugang:	Volltext
Tags:	Tag hinzufügen Keine Tags, Fügen Sie den ersten Tag hinzu!

Schreiben Sie den ersten Kommentar!