Biomolecular condensates are membrane-less assemblies consisting of proteins and nucleic acids. Altered protein dynamics can however lead to pathogenic condensates linked to several neurodegenerative diseases. Numerous studies have reported Liquid-Liquid Phase Separation (LLPS) to be the key mechanism resulting in the formation of biomolecular con- densates. During LLPS, a homogeneous mixture spontaneously separates into a dilute and a dense phase and which then coexist. Computational techniques help us in understanding the dynamics behind protein phase separation. &alpha-Synuclein is an intrinsically disordered protein consisting of 140-residues whose aggregated states are associated with Parkinson&rsquos disease. Sequence of amino acids play a vital role in modulating its phase behavior. In this work, the phase behaviour of P1 (residues 36-42) region, a 7 residue segment from the N-terminal of &alpha-Synuclein is studied. All-atom molecular dynamic simulations at varying temperatures have been conducted to assess the phase change. This study will aid in further understanding the role of different domains of a-Synuclein in phase separation.