Now showing items 1-3 of 3

  • Development of NMR Methodologies to Study Site Specific Zinc-Protein Interactions 

    Benton, Amy Musgrave (East Carolina University, 2021-07-26)
    Found in all three biological domains of life and the second most abundant metal in the human body, zinc (Zn2+) is essential to various cellular processes like the metabolism of DNA and RNA, gene expression, and the ...
  • NMR characterizations of an amyloidogenic conformational ensemble of the PI3K SH3 domain 

    Ahn, Hee-Chul; Le, Yen T. H.; Nagchowdhuri, Partha S.; Derose, Eugene F.; Putnam-Evans, Cindy; London, Robert E.; Markley, John L.; Lim, Kwang Hun (East Carolina University, 2006-11)
    Amyloid formation is associated with structural changes of native polypeptides to monomeric intermediate states and their self-assembly into insoluble aggregates. Characterizations of the amyloidogenic intermediate state ...
  • The RXR-alpha C-terminus T462 is a NMR sensor for coactivator peptide binding 

    Lu, Jianyun; Chen, Minghe; DeKoster, Gregory T.; Cistola, David; Li, Ellen (East Carolina University, 2008-02-22)
    The C-terminal activation function-2 (AF-2) helix plays a crucial role in retinoid X receptor alpha (RXRα)-mediated gene expression. Here, we report a nuclear magnetic resonance (NMR) study of the RXRα ligand-binding domain ...