Mikael Borg

Mikael Borg technical coordinator

coordination, infrastructure

mikael.borg@bils.se
+46 (0)76 306 50 80
https://orcid.org/0000-0002-0646-4231

Mikael Borg earned his PhD in physics at Lund University and has worked as a postdoc in biochemistry, computational biology and bioinformatics at the University of Toronto and at Copenhagen University.

Selected publications

Borg, M., Hamelryck, T., and Ferkinghoff-Borg, J. (2012) On the Physical Relevance and Statistical Interpretation of Knowledge-Based Potentials. In, Hamelryck,T., Mardia,K.V., and Ferkinghoff-Borg,J. (eds), Bayesian Methods in Structural Bioinformatics, Statistics for Biology and Health. Springer Berlin Heidelberg, pp. 97–124.

Borg, M., Mittag, T., Pawson, T., Tyers, M., Forman-Kay, J. D., and Chan, H.-S. (2007) Poly-electrostatic interactions of disordered ligands suggest a physical basis for ultrasensitivity. Proc Natl Acad Sci U S A, 104, 9650–9655.

Hamelryck*, T., Borg*, M., Paluszewski*, M., Paulsen, J., Frellsen, J., Andreetta, C., Boomsma, W., Bottaro, S., and Ferkinghoff-Borg, J. (2010) Potentials of Mean Force for Protein Structure Prediction Vindicated, Formalized and Generalized. PLoS ONE, 5, e13714.

Harder, T., Borg, M., Boomsma, W., Røgen, P., and Hamelryck, T. (2012) Fast large-scale clustering of protein structures using Gauss integrals. Bioinformatics, 28, 510–515.

Harder, T., Borg, M., Bottaro, S., Boomsma, W., Olsson, S., Ferkinghoff-Borg, J., and Hamelryck, T. (2012) An efficient null model for conformational fluctuations in proteins. Structure, 20, 1028–1039.

Kimber*, M. S., Yu*, A. Y., Borg*, M., Leung, E., Chan, H. S., and Houry, W. A. (2010) Structural and theoretical studies indicate that the cylindrical protease ClpP samples extended and compact conformations. Structure, 18, 798–808.

Murphy, J. M., Hansen, D. F., Wiesner, S., Muhandiram, D. R., Borg, M., Smith, M. J., Sicheri, F., Kay, L. E., Forman-Kay, J. D., and Pawson, T. (2009) Structural studies of FF domains of the transcription factor CA150 provide insights into the organization of FF domain tandem arrays. J. Mol. Biol., 393, 409–424.