Abstract
Information about the protein dynamics of myoglobin obtained by x-ray and Mossbauer investigations is analyzed and compared with computer simulations. Computer simulations give correct amplitudes of mean-square displacements but fail in the description of the time dependence of motions. Our model describes protein dynamics at physiological temperatures as an overdamped diffusion-like motion in a restricted space. The fluctuations occur around the average conformation determined by x-ray structure analysis. The gain in entropy drives the molecule into the transition state and, in this way, accounts for its flexibility.
| Originalsprache | Englisch |
|---|---|
| Seiten (von - bis) | 7088-7092 |
| Seitenumfang | 5 |
| Fachzeitschrift | Proceedings of the National Academy of Sciences of the United States of America |
| Jahrgang | 81 |
| Ausgabenummer | 22 I |
| DOIs | |
| Publikationsstatus | Veröffentlicht - 1984 |
| Extern publiziert | Ja |