| 000 | 01286 a2200337 4500 | ||
|---|---|---|---|
| 005 | 20250513202856.0 | ||
| 264 | 0 | _c20000323 | |
| 008 | 200003s 0 0 eng d | ||
| 022 | _a0027-8424 | ||
| 024 | 7 |
_a10.1073/pnas.97.4.1525 _2doi |
|
| 040 |
_aNLM _beng _cNLM |
||
| 100 | 1 | _aFersht, A R | |
| 245 | 0 | 0 |
_aTransition-state structure as a unifying basis in protein-folding mechanisms: contact order, chain topology, stability, and the extended nucleus mechanism. _h[electronic resource] |
| 260 |
_bProceedings of the National Academy of Sciences of the United States of America _cFeb 2000 |
||
| 300 |
_a1525-9 p. _bdigital |
||
| 500 | _aPublication Type: Journal Article | ||
| 650 | 0 | 4 | _aAlgorithms |
| 650 | 0 | 4 | _aAnimals |
| 650 | 0 | 4 | _aDiffusion |
| 650 | 0 | 4 | _aKinetics |
| 650 | 0 | 4 | _aModels, Theoretical |
| 650 | 0 | 4 | _aMutation |
| 650 | 0 | 4 | _aProtein Folding |
| 650 | 0 | 4 |
_aProtein Precursors _xchemistry |
| 650 | 0 | 4 | _aProtein Structure, Secondary |
| 650 | 0 | 4 |
_aSpectrin _xchemistry |
| 650 | 0 | 4 | _aThermodynamics |
| 650 | 0 | 4 | _asrc Homology Domains |
| 773 | 0 |
_tProceedings of the National Academy of Sciences of the United States of America _gvol. 97 _gno. 4 _gp. 1525-9 |
|
| 856 | 4 | 0 |
_uhttps://doi.org/10.1073/pnas.97.4.1525 _zAvailable from publisher's website |
| 999 |
_c10631835 _d10631835 |
||