Robert Huber
Max Planck Institute of Biochemistry
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Primary Section: 21, Biochemistry Membership Type:
International Member
(elected 1995)
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Research Interests
I am particularly interested in the structure of biological molecules with the aim to better understand their function. In my laboratory such structures are studied mainly by x-ray crystallography and more recently also by electron microscopy and nuclear magnetic resonance. We also developed and improved methods to combine information from different sources to facilitate the crystallographic analysis. I began my studies of protein structures with a small natural protease inhibitor BPTI and discovered its substrate-like binding mode seen later in most other inhibitors. This work led to studies of proteolytic enzymes, first digestive enzymes, later enzymes involved in blood clotting and lysosomal and intracellular protein degradation. These structures are of substantial medical importance for drug design and development. In our work on antibody structures we discovered large-scale flexibility in the crystalline state and presented evidence for similar phenomena also in other systems. Interconversion between flexible and rigid structures provides a mechanism for regulation of enzyme activity. Structural studies of bacterial protein complexes related to photosynthesis, light harvesting, and charge separation revealed the physical basis of light absorption, excitation energy transfer, and its transformation into electrical energy. These reactions are among the fastest known in biology and they excel by their quantum efficiency of one. Lately we analyzed very large protein assemblies, like the Proteasome, Riboflavin synthase, GTP cyclohydrolase, and explore methods of ab initio phase determination of the x-ray diffraction data by information obtained from electron microscopy.
