Jeffrey Gray: How Proteins Dance with Their Partners |
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Giddens Inaugural Professorial Lecture, "How Proteins Dance with Their Partners" by Professor Jeffrey Gray.
September 24, 2015 Mason Hall Auditorium 00:00:20 Introductory Remarks by Dean Schlesinger 00:02:38 Remarks from Department Chair Dr. Konstantopoulos 00:04:17 Introduction by Dr. Roger Bonnecaze, University of Texas 00:09:15 Professor Jeff Gray, "How Proteins Dance with Their Parthers" 00:55:23 Q&A Session 01:02:14 Inaugural Professorial Lecture Plaque Presentation Jeffrey Gray, professor in the Department of Chemical and Biomolecular Engineering at the Whiting School of Engineering, presents his Inaugural Professorial Lecture in Mason Hall Auditorium on the Johns Hopkins University’s Homewood campus. Gray’s lecture continues a Whiting School tradition begun in 1993 to honor newly promoted full professors through this special lecture series. Professor Don Giddens, originator of the series, served from 1992 to 1997 as the fifth dean of Engineering at Johns Hopkins University. Abstract: Proteins often are called "the building blocks of life." Protein interactions underlie most biological processes and mechanisms, from proliferation signals in cancer to aggregation events in Parkinson's and Alzheimer's disease to genetic disorders such as Hirschsprung's disease. Encoded by genes, proteins perform much of the work of the cell through binding, recognition, signaling, mechanics, and structure formation. This lecture describes how computational tools can reveal interfaces that allow proteins to accomplish their exquisite functions in the dance of life. Protein docking algorithms can be used to study the atomic structure of the protein interfaces, to explain not only how biological and disease processes work, but also how one might go about altering these processes at the molecular level. Creating computational tools first requires solving problems of basic science, including (10) how to sample the myriad conformations available to proteins and (2) how to accurately calculate the energy of each conformation. A key focus is in modeling antibodies, the workhorses of the immune system, which recognize and remember the specific pathogens that a person has encountered over his or her lifetime. The fastest-growing class of drugs, antibodies act as "smart missiles" by homing in on and binding to particular targets in the body. Current antibody drugs address arthritis, cancer, and heart disease. Algorithms can be used to create reliable structures of antibody-antigen complexes. These tools have a number of practical applications from medicine to biotechnology and molecular detection. In addition, protein-surface research delves into the process by which bones and teeth are formed. In an application to so-called "soft bones" disease, in which babies are born without mineral tissue, a modeled peptide helps restore babies' healthy bone structure. Similar principles inform peptide designs to guide atom-to-atom assembly of nanostructured materials for electronics and energy applications. |