These observations reveal a rapid backward motion at the beginning of each new pulse, which plays a central role in the separation. The measurements are also used to test various models for the physics of gel electrophoresis. Rotating the polarization by 90 switches changes image highlights to into shadows and vice versa. Measurements of the absorption, scattering and fluorescence of macromolecules are made.
New information regarding macromolecular structure leads to new insight concerning their function.
The use of these biophysical techniques are being applied to the study of the kinetics and mechanism of sickle cell hemoglobin depolymerization. When the hemoglobin polymerizes the red blood cell becomes rigid and leads to microvascular occlusion that is responsible for much morbidity and mortality. Another more recent application in this laboratory to sickle hemoglobin has been in an effort to understand how the drug, hydroxyurea - now being prescribed to patients, is working. This project involves rheological measurements and various forms of spectroscopy. EPR which detects unpaired magnetic moments is ideal for studying damage resulting from exposure of keratin proteins to ionizing X-rays or UV light.