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NMR is the method of choice in studying unfolded proteins, as well as proteins such as the prion protein that have highly disordered parts. Since many of the entries in the published genomes appear to code for proteins that should be intrinsically unstructured, an understanding of the nature and behavior of unfolded proteins is assuming increasing importance. Many important proteins contain disordered or dynamic regions, making structure determination by X-ray crystallography and cryo-EM difficult. Incorporation of NMR studies into the determination of the structure and function of molecular machines can define not only structures of flexible portions, but can give insights into the role of molecular motions and disorder into the function of the machine. We have used such a combined approach to examine the complexes of the transcriptiion factor NF-kappaB with DNA and with its inhibitor IkappaB. These studies have led to new insights into the mechanisms by which NF-kappaB transcriptional activation is turned on and off. Another major emphasis in the lab is on the interactions of chaperones with their client proteins and co-chaperones. Again a combined approach using NMR gives new information on these dynamic and heterogeneous systems.
NMR is the method of choice in studying unfolded proteins, as well as proteins such as the prion protein that have highly disordered parts. Since many of the entries in the published genomes appear to code for proteins that should be intrinsically unstructured, an understanding of the nature and behavior of unfolded proteins is assuming increasing importance. Many important proteins contain disordered or dynamic regions, making structure determination by X-ray crystallography and cryo-EM difficult. Incorporation of NMR studies into the determination of the structure and function of molecular machines can define not only structures of flexible portions, but can give insights into the role of molecular motions and disorder into the function of the machine. We have used such a combined approach to examine the complexes of the transcriptiion factor NF-kappaB with DNA and with its inhibitor IkappaB. These studies have led to new insights into the mechanisms by which NF-kappaB transcriptional activation is turned on and off. Another major emphasis in the lab is on the interactions of chaperones with their client proteins and co-chaperones. Again a combined approach using NMR gives new information on these dynamic and heterogeneous systems.
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ISRAEL JOURNAL OF CHEMISTRYno. 10-11 (2023)
H. Jane Dyson, Xiyan Sun
Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature (2023)
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Proceedings of the National Academy of Sciences of the United States of Americano. 47 (2023): e2313835120-e2313835120
JOURNAL OF PHYSICAL CHEMISTRY B (2022)
Journal of molecular biologyno. 11 (2022): 167860-167860
BIOCHEMISTRYno. 23 (2022): 2709-2719
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