Feitelson J, Yedgar S
Department of Physical Chemistry, Hebrew University of Jerusalem, Israel.
Biorheology. 1991;28(1-2):99-105. doi: 10.3233/bir-1991-281-210.
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 protoporphyrin 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 increasing solvent viscosity. This suggests that the fluctuations on the protein structure, which make the above migration possible, are affected by the solvent macroviscosity.
小分子通过蛋白质结构的迁移速率可通过猝灭位于蛋白质内的激发光学探针发出的光来监测。在本研究中，我们研究了溶剂粘度对猝灭剂蒽醌磺酸盐通过肌红蛋白向蛋白质结合位点处激发的锌原卟啉分子迁移速率的影响。通过添加不同分子量的葡聚糖但形成等粘度溶液来增加溶剂粘度。结果表明，蛋白质中的迁移速率随溶剂粘度的增加而降低。这表明使上述迁移成为可能的蛋白质结构波动受到溶剂宏观粘度的影响。
