| 000 | 01722 a2200505 4500 | ||
|---|---|---|---|
| 005 | 20250513205759.0 | ||
| 264 | 0 | _c20000503 | |
| 008 | 200005s 0 0 eng d | ||
| 022 | _a0022-2836 | ||
| 024 | 7 |
_a10.1006/jmbi.2000.3618 _2doi |
|
| 040 |
_aNLM _beng _cNLM |
||
| 100 | 1 | _aKortemme, T | |
| 245 | 0 | 0 |
_aSimilarities between the spectrin SH3 domain denatured state and its folding transition state. _h[electronic resource] |
| 260 |
_bJournal of molecular biology _cApr 2000 |
||
| 300 |
_a1217-29 p. _bdigital |
||
| 500 | _aPublication Type: Journal Article; Research Support, Non-U.S. Gov't | ||
| 650 | 0 | 4 |
_aAcids _xpharmacology |
| 650 | 0 | 4 | _aAmino Acid Sequence |
| 650 | 0 | 4 |
_aAmino Acid Substitution _xgenetics |
| 650 | 0 | 4 | _aAnimals |
| 650 | 0 | 4 | _aChickens |
| 650 | 0 | 4 |
_aDeuterium _xmetabolism |
| 650 | 0 | 4 | _aDrosophila Proteins |
| 650 | 0 | 4 | _aHydrogen-Ion Concentration |
| 650 | 0 | 4 |
_aInsect Proteins _xchemistry |
| 650 | 0 | 4 | _aKinetics |
| 650 | 0 | 4 | _aModels, Molecular |
| 650 | 0 | 4 | _aMolecular Sequence Data |
| 650 | 0 | 4 |
_aMutation _xgenetics |
| 650 | 0 | 4 | _aNuclear Magnetic Resonance, Biomolecular |
| 650 | 0 | 4 |
_aProtein Denaturation _xdrug effects |
| 650 | 0 | 4 | _aProtein Folding |
| 650 | 0 | 4 | _aProtein Renaturation |
| 650 | 0 | 4 |
_aProtein Structure, Secondary _xdrug effects |
| 650 | 0 | 4 | _aProtons |
| 650 | 0 | 4 |
_aSpectrin _xchemistry |
| 650 | 0 | 4 | _aThermodynamics |
| 650 | 0 | 4 |
_asrc Homology Domains _xdrug effects |
| 700 | 1 | _aKelly, M J | |
| 700 | 1 | _aKay, L E | |
| 700 | 1 | _aForman-Kay, J | |
| 700 | 1 | _aSerrano, L | |
| 773 | 0 |
_tJournal of molecular biology _gvol. 297 _gno. 5 _gp. 1217-29 |
|
| 856 | 4 | 0 |
_uhttps://doi.org/10.1006/jmbi.2000.3618 _zAvailable from publisher's website |
| 999 |
_c10717787 _d10717787 |
||