This summer, the Outreach Program takes its cue from President Paul Nurse's 2007 Holiday Lecture, Five Great Ideas of Biology. By examining Life as Chemistry and the emerging idea of Biological Organization, we will explore the chemistry underpinning advances in biomedical research and how structure relates to function. Scientists are just beginning to be able to look at systems and how cells synthesize complex, macromolecular machines such as ion channels (MacKinnon) and nuclear pore complexes (Chait & Rout). Digital documents can be accessed in the Markus Library and on the University network.

June 30 - Seminar immediately follows Orientation. Title: TBD

Roderick MacKinnon, M.D., John D. Rockefeller, Jr., Professor
Investigator, Howard Hughes Medical Institute
Head, Laboratory of Molecular Neurobiology and Biophysics

Roderick MacKinnon shared the 2003 Nobel Prize in Chemistry for his groundbreaking discoveries about the architecture and function of ion channels. His ongoing studies of ion–channel structure are providing important insights into precisely how these molecular machines work-information that may be key to developing new therapeutics for a broad range of disorders, including epilepsy, diabetes, heart arrhythmias, and asthma.

Because this seminar immediately follows Orientation, a journal article will not be associated with the presentation beforehand. However, you may access his Nobel Lecture, Potassium Channels and the Atomic Basis of Selective Ion Conduction.

July 7 - Title: Protein Ligation: An Enabling Technology for the Biophysical Analysis of Proteins

Tom Muir, Ph.D., Richard E. Salomon Professor
Head, Selma and Lawrence Ruben Laboratory of Synthetic Protein Chemistry
Director, Pels Family Center for Biochemistry and Structural Biology

Combining the tools of synthetic chemistry with those of molecular biology and structural biology, Dr. Muir explores the chemical basis of protein function. A major aim of his work is to devise simpler, faster, and more powerful methods for tailor-making proteins. Dr. Muir has been the recipient of several honors, including an Irma T. Hirschl Career Scientist Award and an Irving Sigal Young Investigator Award from the Protein Society.

Muralidharan, V. & Muir, T.W. Protein ligation: an enabling technology for the biophysical analysis of proteins. Nature Methods 3, 429-438 (2006).

July 14 - Title: Using Phage Lytic Enzymes to Control Pathogenic Bacteria

Vincent Fischetti, Ph.D., Professor
Head, Laboratory of Bacterial Pathogenesis and Immunology

Vincent Fischetti, a microbiologist, specializes in the study of gram-positive bacteria, which include such pathogens as the streptococcus, staphylococcus, and anthrax bacteria. Dr. Fischetti has developed an innovative antibacterial strategy to isolate viral enzymes called lysins, which punch lethal holes in viral-infected bacteria. In 2002, the Fischetti group announced the discovery of a lysin that specifically attacks and kills anthrax bacteria. A physical model of this lysin was constructed by former Outreach Teacher, Tommie Hata and his Pingry School students in 2007.

Fischetti, V. A. Bacteriophage lytic enzymes: novel anti-infectives. Trends in Microbiology 13, 491-496 (2005).

July 21 - Title: Designer chemical reactions in living cells

Howard Hang, Ph.D., Assistant Professor
Head, Laboratory of Chemical Biology and Microbial Pathogenesis

Dr. Hang, who joined the Rockefeller faculty in February 2007, is interested in the chemical processes that underlie microbial infection. A major focus of his work is the post-translational modification of proteins that are produced by pathogens and their hosts. Post-translational modifications - chemical changes that regulate the stability and activity of proteins - play a key role in infection and immunity. Dr. Hang has developed and refined methods that have the promise to vastly accelerate the progress of research in this area.

Saxon, E. & Bertozzi, C. R. Cell surface engineering by a modified Staudinger reaction. Science 287, 2007-2010 (2000).

July 28 - Title: The Nuclear Pore Complex: An Extraordinary Machine

Brian Chait, D.Phil., Camille and Henry Dreyfus Professor
Head, Laboratory of Mass Spectrometry and Gaseous Ion Chemistry
&
Michael Rout, Ph.D., Associate Professor
Head, Laboratory of Cellular and Structural Biology

Brian Chait is a world leader in the development of mass spectrometry for the study of biological molecules - technology that is key to progress in proteomics and many other fields of biomedical research. In addition to heading his Rockefeller laboratory, he also directs a National Resource for the Mass Spectrometric Analysis of Biological Macromolecules, located at Rockefeller and funded by the National Institutes of Health. In 2002, Dr. Chait received the American Chemical Society's Frank H. Field and Joe L. Franklin Award for Outstanding Achievement in Mass Spectrometry.

Using a variety of biochemical techniques, Michael Rout has focused on elucidating the structure and mechanism of nuclear pore complexes (NPCs), membranes that act as gatekeepers to regulate the passage of materials into and out of a cell's nucleus. Dr. Rout, working with Dr. Chait and former Rockefeller Professor Andrej Sali, recently published a groundbreaking report revealing the first detailed molecular structure of a nuclear pore complex - the result of a near decade-long collaboration. With support from the NIH, Dr. Rout has also formed the National Center for Dynamic Interactome Research, which he currently heads.

Chait & Rout have selected two journal articles as background for their presentation.
See also Newswire article with video.

Alber, F., Dokudovskaya, S., Veenhoff, L. M., Zhang, W., Kipper, J., Devos, D., Suprapto, A., Karni-Schmidt, O., Williams, R., Chait, B. T., Rout, M. P., & Sali, A. Determining the architectures of macromolecular assemblies. Nature 450, 683-694 (2007).

Alber, F., Dokudovskaya, S., Veenhoff, L. M., Zhang, W., Kipper, J., Devos, D., Suprapto, A., Karni-Schmidt, O., Williams, R., Chait, B. T., Rout, M. P., & Sali, A. The molecular architectures of the nuclear pore complex. Nature 450, 695-701 (2007).

August 4 - Title: Architecture of a coat for the nuclear pore membrane.

Kuo-Chiang Hsia, MS in Biochemistry, National Yang-Ming University, Taiwan
Graduate Fellow, Laboratory of Cell Biology

Kuo-Chiang Hsia came to Rockefeller as a graduate fellow at 2005 having published several papers regarding structures and functions of bacteria nucleases before joining the Laboratory of Cell Biology headed by Günter Blobel, Ph.D., John D. Rockefeller Professor, HHMI Investigator, and Nobel laureate.

Currently, he is trying to combine X-ray crystallography, biochemistry and cell biology skills to understand the structures and functions of nuclear pore complex (NPC), which is one of the most complicated and biggest transporting machines inside the cells. Kuo is first author on today's accompanying journal article for research done in collaboration with Graduate Fellow Peter Stavropoulos, Blobel, and Research Associate Andre Hoelz.

Hsia, Kuo-Chiang, Stavropoulos, P., Blobel, G. & Hoelz, A. Architecture of a coat for the nuclear pore membrane. Cell 131, 1313-1326 (2007). DOI 10.1016/j.cell.2007.11.038

Newswire article.