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.
| Original language | English |
|---|---|
| Pages (from-to) | 7088-7092 |
| Number of pages | 5 |
| Journal | Proceedings of the National Academy of Sciences of the United States of America |
| Volume | 81 |
| Issue number | 22 I |
| DOIs | |
| State | Published - 1984 |
| Externally published | Yes |