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| Name |
Berger, James M. |
| Location
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Johns Hopkins University School of Medicine |
| Primary Field
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Biochemistry |
| Secondary Field
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Biophysics and Computational Biology |
 Election Citation
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Berger's research has provided unprecedented atomic resolution insights into how the energy of ATP hydrolysis is transduced into physiologically relevant work, and how nucleic-acid dependent motors and enzymes function during DNA replication. He is a leader in the study of large macromolecular machines and assemblies. |
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Research Interests
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Berger's research is focused on understanding how multi-subunit assemblies use ATP for overcoming topological challenges within the chromosome and controlling the flow of genetic information. He is particularly interested in developing mechanistic, atomic-level models that explain how macromolecular machines transduce chemical energy into force and motion, and how cells exploit these complexes and their activities to control replisome formation, gene expression, chromosome superstructure, and other essential nucleic-acid transactions. His approaches rely on a variety of structural, biochemical, and biophysical methods to define the architecture, function, evolution, regulation, and small-molecule inhibition of biological complexes. Since starting his independent research program, Berger's group has biochemically and structurally defined the range and nature of a number of key architectural transitions and the physical consequences of nucleotide binding in systems such as topoisomerases, helicases, condensins, and replication initiators. Berger has also successfully determined how many of these enzymes distinguish between DNA substrates and they are controlled by both cellular factors and therapeutic agents. |
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