Showing 1-12 of 12 Results
Lynette Renae Haberman
Academic and Student Services Coordinator, Sarafan ChEM-H
Current Role at StanfordAcademic and Student Services Coordinator
Aida Habtezion MD MSc.
Professor of Medicine (Gastroenterology and Hepatology)On Leave from 01/05/2021 To 01/04/2023
Current Research and Scholarly InterestsLeukocyte recruitment & immune responses in diseases affecting digestive organs
Associate Professor of Biochemistry
Current Research and Scholarly InterestsScientific breakthroughs often come on the heels of technological advances; advances that expose hidden truths of nature, and provide tools for engineering the world around us. Examples include the telescope (heliocentrism), the Michelson interferometer (relativity) and recombinant DNA (molecular evolution). Our lab explores innovative experimental approaches to problems in molecular biochemistry, focusing on technologies with the potential for broad impact.
Director, Geballe Laboratory for Advanced Materials (GLAM), Professor of Materials Science and Engineering and, by courtesy, of Bioengineering and of Chemical Engineering
Current Research and Scholarly InterestsProtein engineering
Professor of Biochemistry and, by courtesy, of Chemical Engineering and of Chemistry
Current Research and Scholarly InterestsOur research is aimed at understanding the chemical and physical behavior underlying biological macromolecules and systems, as these behaviors define the capabilities and limitations of biology. Toward this end we study folding and catalysis by RNA, as well as catalysis by protein enzymes.
David Mulvane Ehrsam and Edward Curtis Franklin Professor of Chemistry and Professor of Photon Science at SLAC
BioCombining inorganic, biophysical and structural chemistry, Professor Keith Hodgson investigates how structure at molecular and macromolecular levels relates to function. Studies in the Hodgson lab have pioneered the use of synchrotron x-radiation to probe the electronic and structural environment of biomolecules. Recent efforts focus on the applications of x-ray diffraction, scattering and absorption spectroscopy to examine metalloproteins that are important in Earth’s biosphere, such as those that convert nitrogen to ammonia or methane to methanol.
Keith O. Hodgson was born in Virginia in 1947. He studied chemistry at the University of Virginia (B.S. 1969) and University of California, Berkeley (Ph.D. 1972), with a postdoctoral year at the ETH in Zurich. He joined the Stanford Chemistry Department faculty in 1973, starting up a program of fundamental research into the use of x-rays to study chemical and biological structure that made use of the unique capabilities of the Stanford Synchrotron Radiation Lightsource (SSRL). His lab carried out pioneering x-ray absorption and x-ray crystallographic studies of proteins, laying the foundation for a new field now in broad use worldwide. In the early eighties, he began development of one of the world's first synchrotron-based structural molecular biology research and user programs, centered at SSRL. He served as SSRL Director from 1998 to 2005, and SLAC National Accelerator Laboratory (SLAC) Deputy Director (2005-2007) and Associate Laboratory Director for Photon Science (2007-2011).
Today the Hodgson research group investigates how molecular structure at different organizational levels relates to biological and chemical function, using a variety of x-ray absorption, diffraction and scattering techniques. Typical of these molecular structural studies are investigations of metal ions as active sites of biomolecules. His research group develops and utilizes techniques such as x-ray absorption and emission spectroscopy (XAS and XES) to study the electronic and metrical details of a given metal ion in the biomolecule under a variety of natural conditions.
A major area of focus over many years, the active site of the enzyme nitrogenase is responsible for conversion of atmospheric di-nitrogen to ammonia. Using XAS studies at the S, Fe and Mo edge, the Hodgson group has worked to understand the electronic structure as a function of redox in this cluster. They have developed new methods to study long distances in the cluster within and outside the protein. Studies are ongoing to learn how this cluster functions during catalysis and interacts with substrates and inhibitors. Other components of the protein are also under active study.
Additional projects include the study of iron in dioxygen activation and oxidation within the binuclear iron-containing enzyme methane monooxygenase and in cytochrome oxidase. Lab members are also investigating the role of copper in electron transport and in dioxygen activation. Other studies include the electronic structure of iron-sulfur clusters in models and enzymes.
The research group is also focusing on using the next generation of x-ray light sources, the free electron laser. Such a light source, called the LCLS, is also located at SLAC. They are also developing new approaches using x-ray free electron laser radiation to image noncrystalline biomolecules and study chemical reactivity on ultrafast time scales.
Michael R. Howitt
Assistant Professor of Pathology and of Microbiology and Immunology
Current Research and Scholarly InterestsOur lab is broadly interested in how intestinal microbes shape our immune system to promote both health and disease. Recently we discovered that a type of intestinal epithelial cell, called tuft cells, act as sentinels stationed along the lining of the gut. Tuft cells respond to microbes, including parasites, to initiate type 2 immunity, remodel the epithelium, and alter gut physiology. Surprisingly, these changes to the intestine rely on the same chemosensory pathway found in oral taste cells. Currently, we aim to 1) elucidate the role of specific tuft cell receptors in microbial detection. 2) To understand how protozoa and bacteria within the microbiota impact host immunity. 3) Discover how tuft cells modulate surrounding cells and tissue.
Professor of Bioengineering and of Microbiology and Immunology
Current Research and Scholarly InterestsHow do cells determine their shape and grow?
How do molecules inside cells get to the right place at the right time?
Our group tries to answer these questions using a systems biology approach, in which we integrate interacting networks of protein and lipids with the physical forces determined by the spatial geometry of the cell. We use theoretical and computational techniques to make predictions that we can verify experimentally using synthetic, chemical, or genetic perturbations.
Assistant Professor of Bioengineering
Current Research and Scholarly InterestsProtein design: molecular engineering, method development and novel therapeutics
Director of Protein Engineering
BioDr. Adrian Hugenmatter joined ChEM-H in 2021 and is leading the Protein Therapeutics Knowledge Center. Dr. Hugenmatter obtained his PhD in the laboratory of Prof. Donald Hilvert at the Swiss Federal Institute of Zurich (ETH Zurich), where he gained his first experience in enzymology, antibody engineering and directed evolution. Fascinated by protein engineering, he joined the laboratory of Prof. Dan Tawfik at the Weizmann Institute of Science (Israel), where he worked on molecular evolution. Dr. Hugenmatter then spent 11 years as a research scientist and team leader at Roche. During that time he developed and optimized several antibody lead candidates for therapeutic application in Oncology and Neuroscience. All along his career, Dr. Hugenmatter was and still is intrigued by the question how a ideal drug must look like to give the maximal benefit to the patient.
Paul S Humphries
Alliance Director, Sarafan ChEM-H
Current Role at StanfordAlliance Director, Stanford Innovative Medicines Accelerator (IMA)