Aurelin Atlas

Aurelin

PDB 2LG4 · NMR

Shenkarev, Z. O., Panteleev, P. V., Balandin, S. V., Gizatullina, A. K., Altukhov, D. A., Finkina, E. I., Kokryakov, V. N., Arseniev, A. S., & Ovchinnikova, T. V. (2012). Recombinant expression and solution structure of antimicrobial peptide aurelin from jellyfish Aurelia aurita. Biochemical and Biophysical Research Communications, 429(1–2), 63–69. doi:10.1016/j.bbrc.2012.10.092 — PDB 2LG4
Ovchinnikova, T. V., Balandin, S. V., Aleshina, G. M., Tagaev, A. A., Leonova, Y. F., Krasnodembsky, E. D., Men'shenin, A. V., & Kokryakov, V. N. (2006). Aurelin, a novel antimicrobial peptide from jellyfish Aurelia aurita with structural features of defensins and channel-blocking toxins. Biochemical and Biophysical Research Communications, 348(2), 514–523. doi:10.1016/j.bbrc.2006.07.078
UniProt Consortium. Aurelin — Q0MWV8 (Swiss-Prot, reviewed).
Gasteiger, E., Hoogland, C., Gattiker, A., Duvaud, S., Wilkins, M. R., Appel, R. D., & Bairoch, A. (2005). Protein identification and analysis tools on the ExPASy server. In The Proteomics Protocols Handbook (pp. 571–607). Humana Press.
Fauchère, J.-L., & Pliška, V. (1983). Hydrophobic parameters π of amino-acid side chains. European Journal of Medicinal Chemistry, 18, 369–375. · Eisenberg, D., Weiss, R. M., & Terwilliger, T. C. (1982). The helical hydrophobic moment. Nature, 299, 371–374.
Bjellqvist, B., Hughes, G. J., Pasquali, C., Paquet, N., Ravier, F., Sanchez, J.-C., Frutiger, S., & Hochstrasser, D. (1993). The focusing positions of polypeptides in immobilized pH gradients. Electrophoresis, 14(1), 1023–1031.
Kyte, J., & Doolittle, R. F. (1982). A simple method for displaying the hydropathic character of a protein. Journal of Molecular Biology, 157(1), 105–132. · Ikai, A. (1980). Thermostability and aliphatic index of globular proteins. Journal of Biochemistry, 88(6), 1895–1898. · Boman, H. G. (2003). Antibacterial peptides: basic facts and emerging concepts. Journal of Internal Medicine, 254(3), 197–215.