000 01505 a2200433 4500
005 20250515015221.0
264 0 _c20060628
008 200606s 0 0 eng d
022 _a0021-9258
024 7 _a10.1074/jbc.M512301200
_2doi
040 _aNLM
_beng
_cNLM
100 1 _aTóth, Júlia
245 0 0 _aThermodynamic analysis reveals structural rearrangement during the acylation step in human trypsin 4 on 4-methylumbelliferyl 4-guanidinobenzoate substrate analogue.
_h[electronic resource]
260 _bThe Journal of biological chemistry
_cMay 2006
300 _a12596-602 p.
_bdigital
500 _aPublication Type: Journal Article; Research Support, Non-U.S. Gov't
650 0 4 _aAcylation
650 0 4 _aBrain
_xmetabolism
650 0 4 _aEntropy
650 0 4 _aGlycine
_xchemistry
650 0 4 _aHot Temperature
650 0 4 _aHumans
650 0 4 _aHydrolysis
650 0 4 _aHymecromone
_xanalogs & derivatives
650 0 4 _aKinetics
650 0 4 _aMolecular Conformation
650 0 4 _aMutation
650 0 4 _aThermodynamics
650 0 4 _aTime Factors
650 0 4 _aTrypsin
_xchemistry
700 1 _aGombos, Linda
700 1 _aSimon, Zoltán
700 1 _aMedveczky, Péter
700 1 _aSzilágyi, László
700 1 _aGráf, László
700 1 _aMálnási-Csizmadia, András
773 0 _tThe Journal of biological chemistry
_gvol. 281
_gno. 18
_gp. 12596-602
856 4 0 _uhttps://doi.org/10.1074/jbc.M512301200
_zAvailable from publisher's website
999 _c16103926
_d16103926