This year’s Nobel Prize in Chemistry was awarded to Venkatraman Ramakrishnan, Ph.D, Thomas A. Steitz, Ph.D., and Ada E. Yonath, Ph.D., for studies of the structure and function of the ribosome. They showed what the ribosome looks like and how it functions at the atomic level. Using x-ray crystallography, they were able to map the position for each and every one of the hundreds of thousands of atoms that make up the ribosome.
Drs. Ramakrishnan, Steitz, and Yonath generated 3-D models that show how different antibiotics bind to the ribosome. These models are now used to develop new antibiotics.
Dr. Ramakrishnan is senior scientist and group leader at structural studies division, MRC Laboratory of Molecular Biology, Cambridge, U.K. He has also worked on the structures of chromatin-related proteins. He continues to delve deeper into the structure and function of the translational machinery, which involves the ribosome and its interaction with mRNA, tRNA, and various protein factors.
Dr. Steitz, is Sterling professor of molecular biophysics and biochemistry and Howard Hughes Medical Institute investigator, both at Yale University. His work is now focusing on establishing the atomic structures of the ribosome captured in the act of protein synthesis in each of its conformational states with elongation factors as well as interacting with the proteins involved in protein secretion.
Dr. Yonath, is Martin S. and Helen Kimmel professor of structural biology and director of Helen & Milton A. Kimmelman Center for Biomolecular Structure & Assembly, both at Weizmann Institute of Science in Israel. In a recent paper, she used controlled heating and an mRNA analog to trigger protein biosynthesis in ribosomal crystals. She then preserved the activated ribosomal crystals using various chemical compounds.