Symmetry-constrained analysis of pulsed double electron-electron resonance (DEER) spectroscopy reveals the dynamic nature of the KcsA activation gate.
Dalmas, Olivier
Symmetry-constrained analysis of pulsed double electron-electron resonance (DEER) spectroscopy reveals the dynamic nature of the KcsA activation gate. [electronic resource] - Journal of the American Chemical Society Oct 2012 - 16360-9 p. digital
Publication Type: Journal Article; Research Support, N.I.H., Extramural
1520-5126
10.1021/ja3069038 doi
Bacterial Proteins--chemistry
Electron Spin Resonance Spectroscopy--methods
Ion Channel Gating
Models, Molecular
Potassium Channels--chemistry
Protein Multimerization
Protein Structure, Quaternary
Protein Structure, Tertiary
Reproducibility of Results
Streptomyces lividans
Symmetry-constrained analysis of pulsed double electron-electron resonance (DEER) spectroscopy reveals the dynamic nature of the KcsA activation gate. [electronic resource] - Journal of the American Chemical Society Oct 2012 - 16360-9 p. digital
Publication Type: Journal Article; Research Support, N.I.H., Extramural
1520-5126
10.1021/ja3069038 doi
Bacterial Proteins--chemistry
Electron Spin Resonance Spectroscopy--methods
Ion Channel Gating
Models, Molecular
Potassium Channels--chemistry
Protein Multimerization
Protein Structure, Quaternary
Protein Structure, Tertiary
Reproducibility of Results
Streptomyces lividans