000			02322 a2200661 4500
005			20250515012942.0
264		0	_c20060510
008			200605s 0 0 eng d
022			_a0021-9258
024	7		_a10.1074/jbc.M512744200 _2doi
040			_aNLM _beng _cNLM
100	1		_aFernández-Sáiz, Vanesa
245	0	0	_aIonic contacts at DnaK substrate binding domain involved in the allosteric regulation of lid dynamics. _h[electronic resource]
260			_bThe Journal of biological chemistry _cMar 2006
300			_a7479-88 p. _bdigital
500			_aPublication Type: Journal Article; Research Support, Non-U.S. Gov't
650	0	4	_aAdenosine Diphosphate _xchemistry
650	0	4	_aAdenosine Triphosphatases _xchemistry
650	0	4	_aAdenosine Triphosphate _xchemistry
650	0	4	_aAllosteric Regulation
650	0	4	_aAllosteric Site
650	0	4	_aAmino Acid Sequence
650	0	4	_aAnisotropy
650	0	4	_aBacterial Proteins _xchemistry
650	0	4	_aBinding Sites
650	0	4	_aCalorimetry, Differential Scanning
650	0	4	_aEscherichia coli _xmetabolism
650	0	4	_aHot Temperature
650	0	4	_aIons
650	0	4	_aKinetics
650	0	4	_aLuciferases _xmetabolism
650	0	4	_aMass Spectrometry
650	0	4	_aMicroscopy, Fluorescence
650	0	4	_aMolecular Chaperones _xchemistry
650	0	4	_aMolecular Conformation
650	0	4	_aMolecular Sequence Data
650	0	4	_aMutagenesis, Site-Directed
650	0	4	_aMutation
650	0	4	_aPeptides _xchemistry
650	0	4	_aProtein Binding
650	0	4	_aProtein Conformation
650	0	4	_aProtein Structure, Secondary
650	0	4	_aProtein Structure, Tertiary
650	0	4	_aSequence Homology, Amino Acid
650	0	4	_aSpectrometry, Mass, Electrospray Ionization
650	0	4	_aSpectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
650	0	4	_aSubstrate Specificity
650	0	4	_aTemperature
650	0	4	_aThermodynamics
650	0	4	_aTime Factors
650	0	4	_aTrypsin _xchemistry
700	1		_aMoro, Fernando
700	1		_aArizmendi, Jesus M
700	1		_aAcebrón, Sergio P
700	1		_aMuga, Arturo
773	0		_tThe Journal of biological chemistry _gvol. 281 _gno. 11 _gp. 7479-88
856	4	0	_uhttps://doi.org/10.1074/jbc.M512744200 _zAvailable from publisher's website
999			_c16031724 _d16031724