The electronic structure of S-layer proteins from Lactobacillus brevis

The valence electronic structure of the S-layer of Lactobacillus brevis is determined using synchrotron-based photoelectron spectroscopy and soft X-ray absorption spectroscopy. Spectra are compared to experimental work on amino-acids and S-layers of Bacillus sphaericus. While it is indeed possible to identify energy levels with those of natural amino-acids, distinct energy shifts are indeed observed which cannot be reconciled using such simple comparisons. Furthermore a strong nitrogen signal observed in both the occupied and unoccupied energy levels suggests that the Lactobacillus brevis protein is amine-terminated. A discussion of the surface of this protein is given. © 2008 IEEE

Keywords

Valence, Electronic structure, Layers, Bacteria, Spectroscopy, Amino acids, Nitrogen, Proteins

Citation

Graham, S. M., Asquith, N. L., Wilde, K., Short, K., Holden, P., Stampfl, A. P. J., Holmes, A. J., Ruys, A., Stojanov, P., Riley, J. D., Fang, L.-J., Yang, Y.-W. & Hwu, Y. (2008). The electronic structure of S-layer proteins from Lactobacillus brevis. In 2008 Conference on Optoelectronic and Microelectronic Materials and Devices, Sydney, NSW, Australia, 28 July-1 August 2008 (pp. 198-201). doi:10.1109/COMMAD.2008.4802125