| Autor: |
Bertini, Ivano, Luchinat, Claudio, Niikura, Yohei, Presenti, Chiara |
| Zdroj: |
Proteins: Structure, Function, and Bioinformatics; October 2000, Vol. 41 Issue: 1 p75-85, 11p |
| Abstrakt: |
15N T1, T2and 1H‐15N NOE were measured for the thermophilic Fe7S8protein from Bacillus schlegeliiand for the Fe4S4HiPIP protein from Chromatium vinosum, which is a mesophilic protein. The investigation was performed at 276, 300, and 330 K at 11.7 T for the former, whereas only the 298 K data at 14.1 T for the latter were acquired. The data were analyzed with the model‐free protocol after correcting the measured parameters for the effect of paramagnetism, because both proteins are paramagnetic. Both thermophilic and mesophilic proteins are quite rigid, with an average value of the generalized order parameter S2at room temperature of 0.92 and 0.94 for Fe7S8and Fe4S4proteins, respectively. The analyzed nitrogens for the Fe7S8protein showed a significant decrease in S2with increasing temperature, and at the highest temperature >70% of the residues had an internal correlation time. This research shows that subnanosecond rigidity is not related to thermostability and provides an estimate of the effect of increasing temperature on this time scale. Proteins 2000;41:75–85. © 2000 Wiley‐Liss, Inc. |
| Databáze: |
Supplemental Index |
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