| 000 | 01666 a2200469 4500 | ||
|---|---|---|---|
| 005 | 20250513205449.0 | ||
| 264 | 0 | _c20000510 | |
| 008 | 200005s 0 0 eng d | ||
| 022 | _a0022-2836 | ||
| 024 | 7 |
_a10.1006/jmbi.2000.3652 _2doi |
|
| 040 |
_aNLM _beng _cNLM |
||
| 100 | 1 | _aBrennan, L | |
| 245 | 0 | 0 |
_aStructural basis for the network of functional cooperativities in cytochrome c(3) from Desulfovibrio gigas: solution structures of the oxidised and reduced states. _h[electronic resource] |
| 260 |
_bJournal of molecular biology _cApr 2000 |
||
| 300 |
_a61-82 p. _bdigital |
||
| 500 | _aPublication Type: Comparative Study; Journal Article; Research Support, Non-U.S. Gov't | ||
| 650 | 0 | 4 | _aAllosteric Regulation |
| 650 | 0 | 4 | _aCalibration |
| 650 | 0 | 4 | _aCrystallography, X-Ray |
| 650 | 0 | 4 |
_aCytochrome c Group _xchemistry |
| 650 | 0 | 4 |
_aDesulfovibrio _xchemistry |
| 650 | 0 | 4 |
_aHeme _xchemistry |
| 650 | 0 | 4 | _aHydrogen Bonding |
| 650 | 0 | 4 | _aHydrogen-Ion Concentration |
| 650 | 0 | 4 | _aModels, Molecular |
| 650 | 0 | 4 | _aMolecular Sequence Data |
| 650 | 0 | 4 | _aNuclear Magnetic Resonance, Biomolecular |
| 650 | 0 | 4 | _aOxidation-Reduction |
| 650 | 0 | 4 | _aProtein Conformation |
| 650 | 0 | 4 | _aSensitivity and Specificity |
| 650 | 0 | 4 | _aSoftware |
| 650 | 0 | 4 | _aSolutions |
| 650 | 0 | 4 | _aStructure-Activity Relationship |
| 700 | 1 | _aTurner, D L | |
| 700 | 1 | _aMessias, A C | |
| 700 | 1 | _aTeodoro, M L | |
| 700 | 1 | _aLeGall, J | |
| 700 | 1 | _aSantos, H | |
| 700 | 1 | _aXavier, A V | |
| 773 | 0 |
_tJournal of molecular biology _gvol. 298 _gno. 1 _gp. 61-82 |
|
| 856 | 4 | 0 |
_uhttps://doi.org/10.1006/jmbi.2000.3652 _zAvailable from publisher's website |
| 999 |
_c10709437 _d10709437 |
||