000			01603 a2200433 4500
005			20250511190653.0
264		0	_c19920929
008			199209s 0 0 eng d
022			_a0006-2960
024	7		_a10.1021/bi00147a022 _2doi
040			_aNLM _beng _cNLM
100	1		_aHarmark, K
245	0	0	_aSubstitution of aspartic acid-80, a residue involved in coordination of magnesium, weakens the GTP binding and strongly enhances the GTPase of the G domain of elongation factor Tu. _h[electronic resource]
260			_bBiochemistry _cAug 1992
300			_a7367-72 p. _bdigital
500			_aPublication Type: Comparative Study; Journal Article; Research Support, Non-U.S. Gov't
650	0	4	_aAmino Acid Sequence
650	0	4	_aAspartic Acid
650	0	4	_aBase Sequence
650	0	4	_aBinding Sites
650	0	4	_aEdetic Acid _xpharmacology
650	0	4	_aGTP Phosphohydrolase-Linked Elongation Factors _xgenetics
650	0	4	_aGuanosine Diphosphate _xmetabolism
650	0	4	_aGuanosine Triphosphate _xmetabolism
650	0	4	_aKinetics
650	0	4	_aMagnesium _xmetabolism
650	0	4	_aModels, Molecular
650	0	4	_aMolecular Sequence Data
650	0	4	_aMutagenesis, Site-Directed
650	0	4	_aOligodeoxyribonucleotides
650	0	4	_aPeptide Elongation Factor Tu _xgenetics
650	0	4	_aProtein Conformation
700	1		_aAnborgh, P H
700	1		_aMerola, M
700	1		_aClark, B F
700	1		_aParmeggiani, A
773	0		_tBiochemistry _gvol. 31 _gno. 32 _gp. 7367-72
856	4	0	_uhttps://doi.org/10.1021/bi00147a022 _zAvailable from publisher's website
999			_c1517409 _d1517409