000 01259 a2200397 4500
005 20250513044526.0
264 0 _c19950213
008 199502s 0 0 eng d
022 _a0006-2960
024 7 _a10.1021/bi00002a010
_2doi
040 _aNLM
_beng
_cNLM
100 1 _aMénard, R
245 0 0 _aModification of the electrostatic environment is tolerated in the oxyanion hole of the cysteine protease papain.
_h[electronic resource]
260 _bBiochemistry
_cJan 1995
300 _a464-71 p.
_bdigital
500 _aPublication Type: Journal Article
650 0 4 _aAnions
650 0 4 _aBase Sequence
650 0 4 _aComputer Simulation
650 0 4 _aElectrochemistry
650 0 4 _aGlutamine
_xchemistry
650 0 4 _aModels, Molecular
650 0 4 _aMolecular Sequence Data
650 0 4 _aMolecular Structure
650 0 4 _aMutagenesis, Site-Directed
650 0 4 _aPapain
_xchemistry
650 0 4 _aRecombinant Proteins
700 1 _aPlouffe, C
700 1 _aLaflamme, P
700 1 _aVernet, T
700 1 _aTessier, D C
700 1 _aThomas, D Y
700 1 _aStorer, A C
773 0 _tBiochemistry
_gvol. 34
_gno. 2
_gp. 464-71
856 4 0 _uhttps://doi.org/10.1021/bi00002a010
_zAvailable from publisher's website
999 _c7818593
_d7818593