| 000 | 01435 a2200409 4500 | ||
|---|---|---|---|
| 005 | 20250514231353.0 | ||
| 264 | 0 | _c20050808 | |
| 008 | 200508s 0 0 eng d | ||
| 022 | _a0022-2836 | ||
| 024 | 7 |
_a10.1016/j.jmb.2005.04.044 _2doi |
|
| 040 |
_aNLM _beng _cNLM |
||
| 100 | 1 | _aOelschlaeger, Peter | |
| 245 | 0 | 0 |
_aHydroxyl groups in the (beta)beta sandwich of metallo-beta-lactamases favor enzyme activity: a computational protein design study. _h[electronic resource] |
| 260 |
_bJournal of molecular biology _cJul 2005 |
||
| 300 |
_a395-401 p. _bdigital |
||
| 500 | _aPublication Type: Journal Article; Research Support, Non-U.S. Gov't | ||
| 650 | 0 | 4 |
_aBacteroides fragilis _xmetabolism |
| 650 | 0 | 4 | _aBinding Sites |
| 650 | 0 | 4 | _aCatalysis |
| 650 | 0 | 4 | _aCircular Dichroism |
| 650 | 0 | 4 | _aComputational Biology |
| 650 | 0 | 4 | _aKinetics |
| 650 | 0 | 4 | _aModels, Molecular |
| 650 | 0 | 4 | _aPoint Mutation |
| 650 | 0 | 4 | _aProtein Folding |
| 650 | 0 | 4 | _aProtein Structure, Secondary |
| 650 | 0 | 4 |
_aProteins _xchemistry |
| 650 | 0 | 4 |
_aProteomics _xmethods |
| 650 | 0 | 4 | _aSoftware |
| 650 | 0 | 4 | _aSubstrate Specificity |
| 650 | 0 | 4 | _aTemperature |
| 650 | 0 | 4 |
_aZinc _xchemistry |
| 650 | 0 | 4 |
_abeta-Lactamases _xchemistry |
| 700 | 1 | _aMayo, Stephen L | |
| 773 | 0 |
_tJournal of molecular biology _gvol. 350 _gno. 3 _gp. 395-401 |
|
| 856 | 4 | 0 |
_uhttps://doi.org/10.1016/j.jmb.2005.04.044 _zAvailable from publisher's website |
| 999 |
_c15606423 _d15606423 |
||