000 01378 a2200349 4500
005 20250516110931.0
264 0 _c20130228
008 201302s 0 0 eng d
022 _a1520-5126
024 7 _a10.1021/ja3069038
_2doi
040 _aNLM
_beng
_cNLM
100 1 _aDalmas, Olivier
245 0 0 _aSymmetry-constrained analysis of pulsed double electron-electron resonance (DEER) spectroscopy reveals the dynamic nature of the KcsA activation gate.
_h[electronic resource]
260 _bJournal of the American Chemical Society
_cOct 2012
300 _a16360-9 p.
_bdigital
500 _aPublication Type: Journal Article; Research Support, N.I.H., Extramural
650 0 4 _aBacterial Proteins
_xchemistry
650 0 4 _aElectron Spin Resonance Spectroscopy
_xmethods
650 0 4 _aIon Channel Gating
650 0 4 _aModels, Molecular
650 0 4 _aPotassium Channels
_xchemistry
650 0 4 _aProtein Multimerization
650 0 4 _aProtein Structure, Quaternary
650 0 4 _aProtein Structure, Tertiary
650 0 4 _aReproducibility of Results
650 0 4 _aStreptomyces lividans
700 1 _aHyde, H Clark
700 1 _aHulse, Raymond E
700 1 _aPerozo, Eduardo
773 0 _tJournal of the American Chemical Society
_gvol. 134
_gno. 39
_gp. 16360-9
856 4 0 _uhttps://doi.org/10.1021/ja3069038
_zAvailable from publisher's website
999 _c22075465
_d22075465