Stanford ChEM-H


Showing 1-8 of 8 Results

  • Daniel Herschlag

    Daniel Herschlag

    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.

  • Pehr Harbury

    Pehr Harbury

    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.

  • Aida Habtezion MD MSc.

    Aida Habtezion MD MSc.

    Associate Professor of Medicine (Gastroenterology and Hepatology)

    Current Research and Scholarly InterestsLeukocyte recruitment & immune responses in diseases affecting digestive organs

  • Sarah Heilshorn

    Sarah Heilshorn

    Associate Professor of Materials Science and Engineering and, by courtesy, of Chemical Engineering and of Bioengineering

    Current Research and Scholarly InterestsProtein engineering
    Tissue engineering
    Regenerative medicine
    Biomaterials

  • Keith Hodgson

    Keith Hodgson

    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.

  • Ngan Huang

    Ngan Huang

    Assistant Professor of Cardiothoracic Surgery (Cardiothoracic Surgery Research)

    Current Research and Scholarly InterestsDr. Huang’s laboratory aims to understand the chemical and mechanical interactions between extracellular matrix (ECM) proteins and pluripotent stem cells that regulate vascular and myogenic differentiation. The fundamental insights of cell-matrix interactions are applied towards stem cell-based therapies with respect to improving cell survival and regenerative capacity, as well as engineered vascularized tissues for therapeutic implantation.

  • KC Huang

    KC Huang

    Associate 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.