We aim to release all our work as pre-prints. This is thus the most up-to-date view of our science. Comments appreciated.

Still unpublished pre-prints:

Karlsson, E.,  Andersson, E., Jones, N.C.,  Vrønning Hoffmann, S.,  Jemth, P. and Kjaergaard, M. (2019) Helix formation during the coupled binding and folding of intrinsically disordered proteins monitored by synchrotron-radiation circular dichroism spectroscopy. bioRxiv

Jendroszek, A. and Kjaergaard M. (2019) Nanoscale spatial dependence of avidity in an IgG1 antibody. bioRxiv

Sørensen, C.S., Jendroszek, A. and Kjaergaard M. (2019) Linker dependence of avidity in multivalent interactions between disordered proteins. bioRxiv

Sørensen, C.S. and Kjaergaard M. (2019) Effective concentrations enforced by intrinsically disordered linkers are governed by polymer physics. bioRxiv

Publications from Aarhus:

Dyla M, Terry DS, Kjaergaard M, Sørensen TL, Lauwring Andersen J, Andersen JP, Rohde Knudsen C, Altman RB, Nissen P, Blanchard SC.  (2017) Dynamics of P-type ATPase transport revealed by single-molecule FRET. Nature. Nov 16;551(7680):346-351.

Kjaergaard, M. and Kragelund B.B. (2017) Functions of intrinsic disorder in transmembrane proteins. Cell Mol Life Sci. Sep;74(17):3205-3224.

Dyla, M., Andersen, J.L., Kjaergaard, M., Birkedal, V., Terry, D.S., Altman, R.B., Blanchard, S.C., Nissen, P., Knudsen, C.R. (2016) Engineering a Prototypic P-type ATPase Listeria monocytogenes Ca2+-ATPase 1 for Single-Molecule FRET Studies. Bioconjug Chem. 2016 21;27(9):2176-87

Kjaergaard, M. (2015) Can a protein be intrinsically disordered inside a membrane? Intrinsically disordered proteins 3(1):1-7

A full publication list including Magnus’s work before moving to Aarhus can be found at ORCID.