000 | 01835 a2200493 4500 | ||
---|---|---|---|
005 | 20250513034038.0 | ||
264 | 0 | _c19950824 | |
008 | 199508s 0 0 eng d | ||
022 | _a0961-8368 | ||
024 | 7 |
_a10.1002/pro.5560040409 _2doi |
|
040 |
_aNLM _beng _cNLM |
||
100 | 1 | _aLowther, W T | |
245 | 0 | 0 |
_aEngineering the substrate specificity of rhizopuspepsin: the role of Asp 77 of fungal aspartic proteinases in facilitating the cleavage of oligopeptide substrates with lysine in P1. _h[electronic resource] |
260 |
_bProtein science : a publication of the Protein Society _cApr 1995 |
||
300 |
_a689-702 p. _bdigital |
||
500 | _aPublication Type: Journal Article; Research Support, U.S. Gov't, P.H.S. | ||
650 | 0 | 4 | _aAmino Acid Sequence |
650 | 0 | 4 | _aAnimals |
650 | 0 | 4 |
_aAspartic Acid _xchemistry |
650 | 0 | 4 |
_aAspartic Acid Endopeptidases _xantagonists & inhibitors |
650 | 0 | 4 | _aBase Sequence |
650 | 0 | 4 | _aCircular Dichroism |
650 | 0 | 4 | _aComputer Graphics |
650 | 0 | 4 |
_aEnzyme Inhibitors _xpharmacology |
650 | 0 | 4 |
_aEnzyme Precursors _xmetabolism |
650 | 0 | 4 | _aHydrogen Bonding |
650 | 0 | 4 | _aHydrogen-Ion Concentration |
650 | 0 | 4 | _aKinetics |
650 | 0 | 4 | _aModels, Molecular |
650 | 0 | 4 | _aMolecular Sequence Data |
650 | 0 | 4 | _aMutagenesis, Site-Directed |
650 | 0 | 4 |
_aOligopeptides _xmetabolism |
650 | 0 | 4 |
_aPepsin A _xchemistry |
650 | 0 | 4 | _aProtein Denaturation |
650 | 0 | 4 | _aProtein Engineering |
650 | 0 | 4 | _aProtein Folding |
650 | 0 | 4 |
_aRecombinant Proteins _xchemistry |
650 | 0 | 4 | _aSubstrate Specificity |
650 | 0 | 4 | _aSwine |
700 | 1 | _aMajer, P | |
700 | 1 | _aDunn, B M | |
773 | 0 |
_tProtein science : a publication of the Protein Society _gvol. 4 _gno. 4 _gp. 689-702 |
|
856 | 4 | 0 |
_uhttps://doi.org/10.1002/pro.5560040409 _zAvailable from publisher's website |
999 |
_c7612904 _d7612904 |