| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 1815851 | Physica B: Condensed Matter | 2006 | 4 Pages |
Abstract
A moment analysis of the self-intermediate scattering function is used to reconstruct the distribution of structural displacements in the small protein myoglobin as a function of time, temperature and environment. Model-independent information is obtained on mean squared displacements and the Gauss-deviation. Two types of molecular motions were identified: rotational jumps of side chains and small-scale translational displacements induced by interfacial water. The displacements of water on the protein surface increase sublinearly with time and the fourth moment deviates from a Gaussian value.
Related Topics
Physical Sciences and Engineering
Physics and Astronomy
Condensed Matter Physics
Authors
Wolfgang Doster,