| 000 | 01826 a2200505 4500 | ||
|---|---|---|---|
| 005 | 20250514010742.0 | ||
| 264 | 0 | _c20020110 | |
| 008 | 200201s 0 0 eng d | ||
| 022 | _a0021-9258 | ||
| 024 | 7 |
_a10.1074/jbc.M106693200 _2doi |
|
| 040 |
_aNLM _beng _cNLM |
||
| 100 | 1 | _aTieman, B C | |
| 245 | 0 | 0 |
_aA comparison of the GroE chaperonin requirements for sequentially and structurally homologous malate dehydrogenases: the importance of folding kinetics and solution environment. _h[electronic resource] |
| 260 |
_bThe Journal of biological chemistry _cNov 2001 |
||
| 300 |
_a44541-50 p. _bdigital |
||
| 500 | _aPublication Type: Comparative Study; Journal Article; Research Support, U.S. Gov't, P.H.S. | ||
| 650 | 0 | 4 | _aAmino Acid Sequence |
| 650 | 0 | 4 | _aAnimals |
| 650 | 0 | 4 |
_aBacterial Proteins _xmetabolism |
| 650 | 0 | 4 |
_aChaperonins _xchemistry |
| 650 | 0 | 4 | _aDose-Response Relationship, Drug |
| 650 | 0 | 4 |
_aEscherichia coli _xenzymology |
| 650 | 0 | 4 | _aEscherichia coli Proteins |
| 650 | 0 | 4 |
_aGlycerol _xpharmacology |
| 650 | 0 | 4 |
_aHeat-Shock Proteins _xmetabolism |
| 650 | 0 | 4 | _aKinetics |
| 650 | 0 | 4 | _aLight |
| 650 | 0 | 4 |
_aMalate Dehydrogenase _xchemistry |
| 650 | 0 | 4 | _aModels, Chemical |
| 650 | 0 | 4 | _aMolecular Sequence Data |
| 650 | 0 | 4 |
_aPlasmids _xmetabolism |
| 650 | 0 | 4 | _aProtein Binding |
| 650 | 0 | 4 | _aProtein Conformation |
| 650 | 0 | 4 | _aProtein Denaturation |
| 650 | 0 | 4 | _aProtein Folding |
| 650 | 0 | 4 | _aScattering, Radiation |
| 650 | 0 | 4 | _aSequence Homology, Amino Acid |
| 650 | 0 | 4 | _aSwine |
| 650 | 0 | 4 | _aTemperature |
| 650 | 0 | 4 | _aTime Factors |
| 700 | 1 | _aJohnston, M F | |
| 700 | 1 | _aFisher, M T | |
| 773 | 0 |
_tThe Journal of biological chemistry _gvol. 276 _gno. 48 _gp. 44541-50 |
|
| 856 | 4 | 0 |
_uhttps://doi.org/10.1074/jbc.M106693200 _zAvailable from publisher's website |
| 999 |
_c11474414 _d11474414 |
||