| 000 | 01528 a2200433 4500 | ||
|---|---|---|---|
| 005 | 20250513212616.0 | ||
| 264 | 0 | _c20001107 | |
| 008 | 200011s 0 0 eng d | ||
| 022 | _a0961-8368 | ||
| 024 | 7 |
_a10.1110/ps.9.5.878 _2doi |
|
| 040 |
_aNLM _beng _cNLM |
||
| 100 | 1 | _aHyre, D E | |
| 245 | 0 | 0 |
_aSer45 plays an important role in managing both the equilibrium and transition state energetics of the streptavidin-biotin system. _h[electronic resource] |
| 260 |
_bProtein science : a publication of the Protein Society _cMay 2000 |
||
| 300 |
_a878-85 p. _bdigital |
||
| 500 | _aPublication Type: Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, P.H.S. | ||
| 650 | 0 | 4 | _aBinding Sites |
| 650 | 0 | 4 |
_aBiotin _xchemistry |
| 650 | 0 | 4 | _aCalorimetry |
| 650 | 0 | 4 | _aCrystallography, X-Ray |
| 650 | 0 | 4 | _aHydrogen Bonding |
| 650 | 0 | 4 | _aKinetics |
| 650 | 0 | 4 | _aMolecular Sequence Data |
| 650 | 0 | 4 | _aMutagenesis |
| 650 | 0 | 4 |
_aPlasmids _xmetabolism |
| 650 | 0 | 4 | _aProtein Binding |
| 650 | 0 | 4 | _aProtein Structure, Secondary |
| 650 | 0 | 4 |
_aSerine _xchemistry |
| 650 | 0 | 4 |
_aStreptavidin _xchemistry |
| 650 | 0 | 4 | _aTemperature |
| 650 | 0 | 4 | _aThermodynamics |
| 650 | 0 | 4 | _aTime Factors |
| 700 | 1 | _aLe Trong, I | |
| 700 | 1 | _aFreitag, S | |
| 700 | 1 | _aStenkamp, R E | |
| 700 | 1 | _aStayton, P S | |
| 773 | 0 |
_tProtein science : a publication of the Protein Society _gvol. 9 _gno. 5 _gp. 878-85 |
|
| 856 | 4 | 0 |
_uhttps://doi.org/10.1110/ps.9.5.878 _zAvailable from publisher's website |
| 999 |
_c10801896 _d10801896 |
||