Thalidomide achieved notoriety 50 years ago because of a wave of birth defects among children born to women who took this drug during pregnancy as a treatment for morning sickness. Thalidomide is a mixture of two enantiomers; one reduces morning sickness, but the other causes severe birth defects. (Although the beneficial enantiomer can be synthesized and given to patients, it is converted in the body to the harmful enantiomer.) The U.S. Food and Drug Administration (FDA) withheld approval of thalidomide in 1960. Since then, however, the FDA has approved this drug for the treatment of conditions associated with Hansens disease (leprosy) and newly diagnosed multiple myeloma, a blood and bone marrow cancer. In clinical trials, thalidomide also shows promise as a treatment for AIDS, tuberculosis, inflammatory diseases, and some other types of cancer. Assuming that molecules related to thalidomide could be synthesized in the laboratory, describe in a broad way the type of experiments you would do to improve the benefits of this drug and minimize its harmful effects.
BIO 130 Regulation of Proteins by phosphorylation turing off a signal is just as important as tunrning it on - each activation step needs to be inactivated - depends on the balance between activities of kinase and phosphatase Phosphorylation is caused by... serine and threonine kinases in particular sequences tyrosine kinases phosphorylate hydroxyl groups GTP Binding proteins -Switch from active to inactive state depending on whether or not they are bound to GTP or GDP - Once bound to GTP the G-proteins have intrinsic GTPase activity, and turn themselves on by hydrolyzing GTP to GDP Cell surface receptors 1 - Binding