000			01766 a2200433 4500
005			20250514230243.0
264		0	_c20050816
008			200508s 0 0 eng d
022			_a0006-2960
024	7		_a10.1021/bi0501636 _2doi
040			_aNLM _beng _cNLM
100	1		_aSilversmith, Ruth E
245	0	0	_aHigh mobility of carboxyl-terminal region of bacterial chemotaxis phosphatase CheZ is diminished upon binding divalent cation or CheY-P substrate. _h[electronic resource]
260			_bBiochemistry _cMay 2005
300			_a7768-76 p. _bdigital
500			_aPublication Type: Journal Article; Research Support, N.I.H., Extramural; Research Support, U.S. Gov't, P.H.S.
650	0	4	_aAmino Acid Sequence
650	0	4	_aBacterial Proteins _xantagonists & inhibitors
650	0	4	_aBeryllium _xmetabolism
650	0	4	_aBinding Sites
650	0	4	_aCations, Divalent _xchemistry
650	0	4	_aChemotaxis
650	0	4	_aEscherichia coli Proteins
650	0	4	_aFluorescein _xmetabolism
650	0	4	_aFluorescence Polarization
650	0	4	_aFluorescence Resonance Energy Transfer
650	0	4	_aFluorides _xmetabolism
650	0	4	_aMagnesium Chloride _xchemistry
650	0	4	_aMembrane Proteins _xantagonists & inhibitors
650	0	4	_aMethyl-Accepting Chemotaxis Proteins
650	0	4	_aMolecular Motor Proteins _xantagonists & inhibitors
650	0	4	_aMolecular Sequence Data
650	0	4	_aPeptide Fragments _xantagonists & inhibitors
650	0	4	_aPhosphoric Monoester Hydrolases _xantagonists & inhibitors
650	0	4	_aProtein Structure, Tertiary
650	0	4	_aSubstrate Specificity
773	0		_tBiochemistry _gvol. 44 _gno. 21 _gp. 7768-76
856	4	0	_uhttps://doi.org/10.1021/bi0501636 _zAvailable from publisher's website
999			_c15571832 _d15571832