| 000 | 01862 a2200517 4500 | ||
|---|---|---|---|
| 005 | 20250513110617.0 | ||
| 264 | 0 | _c19970128 | |
| 008 | 199701s 0 0 eng d | ||
| 022 | _a0027-8424 | ||
| 024 | 7 |
_a10.1073/pnas.93.26.15024 _2doi |
|
| 040 |
_aNLM _beng _cNLM |
||
| 100 | 1 | _aZahn, R | |
| 245 | 0 | 0 |
_aChaperone activity and structure of monomeric polypeptide binding domains of GroEL. _h[electronic resource] |
| 260 |
_bProceedings of the National Academy of Sciences of the United States of America _cDec 1996 |
||
| 300 |
_a15024-9 p. _bdigital |
||
| 500 | _aPublication Type: Journal Article; Research Support, Non-U.S. Gov't | ||
| 650 | 0 | 4 | _aAllosteric Regulation |
| 650 | 0 | 4 |
_aAmino Acid Isomerases _xchemistry |
| 650 | 0 | 4 | _aAmino Acid Sequence |
| 650 | 0 | 4 | _aBase Sequence |
| 650 | 0 | 4 | _aBinding Sites |
| 650 | 0 | 4 |
_aCarrier Proteins _xchemistry |
| 650 | 0 | 4 |
_aChaperonin 60 _xbiosynthesis |
| 650 | 0 | 4 | _aCrystallography, X-Ray |
| 650 | 0 | 4 | _aDNA Primers |
| 650 | 0 | 4 |
_aEscherichia coli _xmetabolism |
| 650 | 0 | 4 | _aKinetics |
| 650 | 0 | 4 | _aModels, Molecular |
| 650 | 0 | 4 | _aMolecular Sequence Data |
| 650 | 0 | 4 |
_aPeptide Fragments _xbiosynthesis |
| 650 | 0 | 4 | _aPeptidylprolyl Isomerase |
| 650 | 0 | 4 | _aPolymerase Chain Reaction |
| 650 | 0 | 4 | _aProtein Denaturation |
| 650 | 0 | 4 | _aProtein Folding |
| 650 | 0 | 4 | _aProtein Structure, Secondary |
| 650 | 0 | 4 |
_aRecombinant Proteins _xbiosynthesis |
| 650 | 0 | 4 |
_aThiosulfate Sulfurtransferase _xchemistry |
| 700 | 1 | _aBuckle, A M | |
| 700 | 1 | _aPerrett, S | |
| 700 | 1 | _aJohnson, C M | |
| 700 | 1 | _aCorrales, F J | |
| 700 | 1 | _aGolbik, R | |
| 700 | 1 | _aFersht, A R | |
| 773 | 0 |
_tProceedings of the National Academy of Sciences of the United States of America _gvol. 93 _gno. 26 _gp. 15024-9 |
|
| 856 | 4 | 0 |
_uhttps://doi.org/10.1073/pnas.93.26.15024 _zAvailable from publisher's website |
| 999 |
_c8978212 _d8978212 |
||