Aggregation of proteins to dimers or higher-order oligomers is in many cases required for their proper function. However, high-resolution structural data is usually only obtained under crystallization conditions, while methods applicable to more physiological environments typically come with low resolution. In the talk I will discuss recent progress in the usage of molecular dynamics simulations in protein oligomerization. Using ensembles of simulations at coarse-grained resolution [1] we show how (i) dimerization of a small soluble protein domain may enable a two-pore channel to adopt a voltage- and Ca2+-sensitive conformation [2], (ii) how synaptobrevin 2 forms dimers and higher-order oligomers probably coupled to membrane fusion [3-6], and (iii) how cholesterol may change the dimerisation pattern of a G protein coupled receptor that is of importance for the activation of the receptor [7].

[1] Wassenaar et al., J. Chem. Theory Comput. 11:2278-2291 (2015)
[2] Larisch et al., Cell. Mol. Life Sci. in press (2016)
[3] Pluhackova et al., J. Phys. Chem. B 119:4396-4408 (2015)
[4] Han et al., Biophys.J. 109:760-771 (2015)
[5] Han et al., BBA-Biomembranes 1858:855-865 (2016)
[6] Han et al., submitted (2016)
[7] Pluhackova et al., submitted (2016)