| 000 | 01396 a2200397 4500 | ||
|---|---|---|---|
| 005 | 20250513083728.0 | ||
| 264 | 0 | _c19960206 | |
| 008 | 199602s 0 0 eng d | ||
| 022 | _a0065-2598 | ||
| 024 | 7 |
_a10.1007/978-1-4615-1871-6_71 _2doi |
|
| 040 |
_aNLM _beng _cNLM |
||
| 100 | 1 | _aTopol, I A | |
| 245 | 0 | 0 |
_aA quantum mechanical model of the hydration and acidity of the active site in aspartic proteases. _h[electronic resource] |
| 260 |
_bAdvances in experimental medicine and biology _c1995 |
||
| 300 |
_a549-54 p. _bdigital |
||
| 500 | _aPublication Type: Comparative Study; Journal Article | ||
| 650 | 0 | 4 | _aAmino Acid Sequence |
| 650 | 0 | 4 |
_aAspartic Acid Endopeptidases _xchemistry |
| 650 | 0 | 4 | _aBinding Sites |
| 650 | 0 | 4 | _aCatalysis |
| 650 | 0 | 4 | _aCrystallography, X-Ray |
| 650 | 0 | 4 | _aElectrochemistry |
| 650 | 0 | 4 | _aHydrogen-Ion Concentration |
| 650 | 0 | 4 | _aMolecular Sequence Data |
| 650 | 0 | 4 | _aMutagenesis, Site-Directed |
| 650 | 0 | 4 | _aPoint Mutation |
| 650 | 0 | 4 | _aProtein Conformation |
| 650 | 0 | 4 | _aQuantum Theory |
| 650 | 0 | 4 |
_aRecombinant Proteins _xchemistry |
| 650 | 0 | 4 | _aThermodynamics |
| 700 | 1 | _aCachau, R E | |
| 700 | 1 | _aBurt, S K | |
| 700 | 1 | _aErickson, J W | |
| 773 | 0 |
_tAdvances in experimental medicine and biology _gvol. 362 _gp. 549-54 |
|
| 856 | 4 | 0 |
_uhttps://doi.org/10.1007/978-1-4615-1871-6_71 _zAvailable from publisher's website |
| 999 |
_c8539471 _d8539471 |
||