000 01744 a2200433 4500
005 20250513213953.0
264 0 _c20001103
008 200011s 0 0 eng d
022 _a0961-8368
024 7 _a10.1110/ps.9.6.1085
_2doi
040 _aNLM
_beng
_cNLM
100 1 _aGinsburg, A
245 0 0 _aConformational stability changes of the amino terminal domain of enzyme I of the Escherichia coli phosphoenolpyruvate: sugar phosphotransferase system produced by substituting alanine or glutamate for the active-site histidine 189: implications for phosphorylation effects.
_h[electronic resource]
260 _bProtein science : a publication of the Protein Society
_cJun 2000
300 _a1085-94 p.
_bdigital
500 _aPublication Type: Journal Article
650 0 4 _aAlanine
_xchemistry
650 0 4 _aAmino Acid Substitution
650 0 4 _aBinding Sites
650 0 4 _aCalorimetry, Differential Scanning
650 0 4 _aEscherichia coli
_xenzymology
650 0 4 _aGlutamic Acid
_xchemistry
650 0 4 _aHistidine
_xchemistry
650 0 4 _aModels, Molecular
650 0 4 _aPhosphoenolpyruvate Sugar Phosphotransferase System
_xchemistry
650 0 4 _aPhosphorylation
650 0 4 _aPhosphotransferases (Nitrogenous Group Acceptor)
_xchemistry
650 0 4 _aProtein Conformation
650 0 4 _aProtein Denaturation
650 0 4 _aThermodynamics
700 1 _aSzczepanowski, R H
700 1 _aRuvinov, S B
700 1 _aNosworthy, N J
700 1 _aSondej, M
700 1 _aUmland, T C
700 1 _aPeterkofsky, A
773 0 _tProtein science : a publication of the Protein Society
_gvol. 9
_gno. 6
_gp. 1085-94
856 4 0 _uhttps://doi.org/10.1110/ps.9.6.1085
_zAvailable from publisher's website
999 _c10843207
_d10843207