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Hermann Schindelin, Ph.D.
Assistant Professor of Biochemistry and Cell Biology.
Funding through the National Institute of Diabetes and Digestive and Kidney
Diseases.
Figure 1. Structure of the MoaC hexamer.
This enzyme is involved in the initial stage of molybdenum cofactor
biosynthesis. The left side shows a ribbon diagram, the right
side a space filling representation. Different shades indicate
the different subunits. |
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Research in our laboratory is aimed at understanding the structural
features of enzymes and the detailed aspects of their catalytic mechanism.
One major research area is focused on enzymes involved in the biosynthesis
of the molybdenum cofactor. This is an evolutionary conserved pathway
also present in humans. Deficiencies of enzymes in this pathway lead to
a severe and deadly disease in humans. We are in the process of solving
the crystal structures of each enzyme involved in this pathway, with the
goal of characterizing their enzymatic mechanisms (Figure 1). We are also
studying enzymes involved in ubiquitin-dependent protein degradation,
considering the initial step of ubiquitin activation and the final step
of substrate identification.
Ideally, IBRP students who wish to contribute to our research endeavors
will have a background in physics or physical chemistry. Familiarity with
computers is also desirable. The student will have several different types
of projects available from which to choose. One involves crystallization
of novel proteins. The student will try to obtain crystals of a protein
of interest through screening methods. If successful, the crystals will
be characterized by crystallographic techniques. A second option is an
analysis of structural features of proteins. The student will use computational
tools to identify regions of interest such as the location of active sites
or unusual structural features by database searches. Finally, a student
may work on the characterization of enzyme properties in solution. The
student will develop and conduct assays to characterize the catalytic
properties of a particular enzyme by kinetic methods or study conformational
changes as a result of ligand binding using spectroscopic techniques such
as circular dichroism and fluorescence spectroscopy.
Student Background: Students interested in learning crystallographic
and biochemical techniques to study the structure and function of enzymes.
Students with a background in Chemistry/Physics and a desire to apply
quantitative techniques to biological problems are encouraged to apply.
Contact Information
email: schindelin@pharm.sunysb.edu
url: http://www.sunysb.edu/biochem/BIOCHEM/facultypages/schindelin/
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