| 000 | 01614 a2200469 4500 | ||
|---|---|---|---|
| 005 | 20250513185352.0 | ||
| 264 | 0 | _c19990805 | |
| 008 | 199908s 0 0 eng d | ||
| 022 | _a0887-3585 | ||
| 040 |
_aNLM _beng _cNLM |
||
| 100 | 1 | _aMunier-Lehmann, H | |
| 245 | 0 | 0 |
_aA new subfamily of short bacterial adenylate kinases with the Mycobacterium tuberculosis enzyme as a model: A predictive and experimental study. _h[electronic resource] |
| 260 |
_bProteins _cAug 1999 |
||
| 300 |
_a238-48 p. _bdigital |
||
| 500 | _aPublication Type: Comparative Study; Journal Article; Research Support, Non-U.S. Gov't | ||
| 650 | 0 | 4 |
_aAdenylate Kinase _xchemistry |
| 650 | 0 | 4 | _aAmino Acid Sequence |
| 650 | 0 | 4 | _aAnimals |
| 650 | 0 | 4 | _aCircular Dichroism |
| 650 | 0 | 4 | _aCloning, Molecular |
| 650 | 0 | 4 | _aEnzyme Stability |
| 650 | 0 | 4 | _aKinetics |
| 650 | 0 | 4 | _aModels, Molecular |
| 650 | 0 | 4 | _aMolecular Sequence Data |
| 650 | 0 | 4 | _aMolecular Weight |
| 650 | 0 | 4 |
_aMycobacterium tuberculosis _xenzymology |
| 650 | 0 | 4 | _aNuclear Magnetic Resonance, Biomolecular |
| 650 | 0 | 4 | _aProtein Denaturation |
| 650 | 0 | 4 | _aProtein Structure, Secondary |
| 650 | 0 | 4 |
_aRecombinant Proteins _xbiosynthesis |
| 650 | 0 | 4 | _aSequence Alignment |
| 650 | 0 | 4 | _aSequence Homology, Amino Acid |
| 650 | 0 | 4 | _aSpectrophotometry, Infrared |
| 650 | 0 | 4 | _aTemperature |
| 650 | 0 | 4 | _aTosylphenylalanyl Chloromethyl Ketone |
| 650 | 0 | 4 |
_aTrypsin _xmetabolism |
| 700 | 1 | _aBurlacu-Miron, S | |
| 700 | 1 | _aCraescu, C T | |
| 700 | 1 | _aMantsch, H H | |
| 700 | 1 | _aSchultz, C P | |
| 773 | 0 |
_tProteins _gvol. 36 _gno. 2 _gp. 238-48 |
|
| 999 |
_c10356637 _d10356637 |
||