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

Conformational Biases of {\alpha}-Synuclein and Formation of Transient Knots