Abstract
The migration rate of small molecules through the structure of proteins can be monitored by quenching the light emitted from an excited optical probe located within the protein. In the present study we examined the influence of the solvent viscosity on the migration rate of the quencher anthraquinone sulfonate through myoglobin towards an excited Zn protoporpohyrin molecule at the binding site of the protein. The solvent viscosity was increased by adding dextrans of different molecular weight but forming isoviscous solutions. The results demonstrate that the migration rate in the protein decreases with solvent increasing viscosity. This suggest that the fluctuationson the protein structure, which make the above migration possible, are affected by the solvent macroviscosity.
| Original language | English |
|---|---|
| Pages (from-to) | 99-105 |
| Number of pages | 7 |
| Journal | Biorheology |
| Volume | 28 |
| Issue number | 1-2 |
| DOIs | |
| State | Published - 1991 |
Keywords
- myoglobin dynamics
- solvent viscosity