  We study local conformational biases in the dynamics of {\alpha}-synuclein by
using all-atom simulations with explicit and implicit solvents. The biases are
related to the frequency of the specific contact formation. In both approaches,
the protein is intrinsically disordered, and its strongest bias is to make bend
and turn local structures. The explicit-solvent conformations can be
substantially more extended which allows for formation of transient trefoil
knots, both deep and shallow, that may last for up to 5 {\mu}s. The two-chain
self-association events, both short- and long-lived, are dominated by formation
of contacts in the central part of the sequence. This part tends to form
helices when bound to a micelle.
