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Cheng Her, Graduate Student

Chang Her

Research Description

My research focus is to elucidate the structural mechanisms associated with the regulation and misregulation of the cardiac calcium release channel, ryanodine receptor (RyR), by calmodulin (CaM). CaM is a calcium-binding protein that regulates RyR function in both skeletal and cardiac muscle. This interaction is altered by oxidation and disease-causing mutations in CaM, which can lead to fatal cardiac arrhythmia. The functional regulation of RyR by CaM is well characterized but the structural details remain unknown. In order to better understand the structural mechanisms behind this interaction, I employ a combination of techniques including solid-phase peptide synthesis, site-directed spin labeling utilizing bifunctional spin labels, and both continuous wave and pulse EPR.


  1. Her C, JE McCaffrey, DD Thomas, and CB Karim. 2016. Calcium-dependent structural dynamics of a spin-labeled ryanodine receptor peptide bound to calmodulin. Biophys. J. 111, 2387-2394.
  2. Lewis AK, K Dunleavy, TL Senkow, C Her, BT Horn, MA Jersett, R Mahling, MR McCarthy, GT Perell, CC Valley, CB Karim, J Gao, WC Pomerantz, DD Thomas, A Cembran, A Hinderliter, and JN Sachs. 2016. Oxidation increases the strength of the methionine-aromatic interaction. Nat. Chem. Biol. 12, 860-866.
  3. Her C, and T Yang. 2015. Synthesis of a cyclic dimer MUC1 mucin peptide and its antibody binding properties revealed by STD-NMR. Am. J. Undergrad. Res. 12, 79-92.
  4. Yang T, C Her, AR Lynch, RJ White, M Wang and WM Westler. 2015. Short proline-substituted MUC1 mucin peptides can bind to mouse MUC1 monoclonal antibody as revealed by STD-NMR. Am. J. Undergrad. Res. 14, 5-11.
  5. Warren, N, A Strom, B Nicolet, K Albin, J Albrecht, B Bausch, M Dobbe, M Dudek, S Firgens, C Fritsche, A Gunderson, J Heimann, C Her, J Hurt, D Konorev, M Lively, S Meacham, V Rodriguez, S Tadayon, D Trcka, Y Yang, S Bhattacharyya and S Hati. 2014. Comparison of the intrinsic dynamics of aminoacyl-tRNA synthetases. Protein J. 33, 184-198.