| 000 | 01284 a2200361 4500 | ||
|---|---|---|---|
| 005 | 20250513142252.0 | ||
| 264 | 0 | _c19980608 | |
| 008 | 199806s 0 0 eng d | ||
| 022 | _a0006-2960 | ||
| 024 | 7 |
_a10.1021/bi9730994 _2doi |
|
| 040 |
_aNLM _beng _cNLM |
||
| 100 | 1 | _aSoloaga, A | |
| 245 | 0 | 0 |
_aReversible denaturation, self-aggregation, and membrane activity of Escherichia coli alpha-hemolysin, a protein stable in 6 M urea. _h[electronic resource] |
| 260 |
_bBiochemistry _cMay 1998 |
||
| 300 |
_a6387-93 p. _bdigital |
||
| 500 | _aPublication Type: Journal Article; Research Support, Non-U.S. Gov't | ||
| 650 | 0 | 4 | _aAmino Acid Sequence |
| 650 | 0 | 4 |
_aBacterial Proteins _xchemistry |
| 650 | 0 | 4 |
_aBacterial Toxins _xchemistry |
| 650 | 0 | 4 |
_aCalcium Chloride _xmetabolism |
| 650 | 0 | 4 | _aCircular Dichroism |
| 650 | 0 | 4 | _aDrug Storage |
| 650 | 0 | 4 | _aEscherichia coli Proteins |
| 650 | 0 | 4 |
_aHemolysin Proteins _xchemistry |
| 650 | 0 | 4 | _aMolecular Sequence Data |
| 650 | 0 | 4 | _aProtein Denaturation |
| 650 | 0 | 4 | _aProtein Structure, Tertiary |
| 650 | 0 | 4 | _aUrea |
| 700 | 1 | _aRamírez, J M | |
| 700 | 1 | _aGoñi, F M | |
| 773 | 0 |
_tBiochemistry _gvol. 37 _gno. 18 _gp. 6387-93 |
|
| 856 | 4 | 0 |
_uhttps://doi.org/10.1021/bi9730994 _zAvailable from publisher's website |
| 999 |
_c9539866 _d9539866 |
||