Abstract
Rapid electron motion in the proteins, cytochrome c and myoglobin has been studied using muon spin relaxation. Measurements between 5 and 300 K show that the inter-site diffusion rate for the topologically 1D motion along the polypeptide chain is only weakly dependent on temperature. Evidence for an increase in higher dimensional motion is seen around 200 K in cytochrome c, apparently reflecting structural change. For myoglobin the variation with temperature is different, reflecting the different protein dynamics of this molecule.
Original language | English |
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Pages (from-to) | 631-635 |
Number of pages | 5 |
Journal | Physica B: Condensed Matter |
Volume | 289-290 |
DOIs | |
Publication status | Published - 2000 Aug |
Externally published | Yes |
Event | 8th International Conference on Muon Spin Rotation, Relaxation and Resonance (muSR'99) - Les Diablerets, Switz Duration: 1999 Aug 30 → 1999 Sept 3 |
ASJC Scopus subject areas
- Electronic, Optical and Magnetic Materials
- Condensed Matter Physics
- Electrical and Electronic Engineering