Chromatin remodeling is essential for gene regulation and DNA repair. Apart from histones, High Mobility Group (HMG) proteins are the most abundant genome-associated proteins present in Saccharomyces cerevisiae. They play a vital role in the assembly and disassembly of chromatin, by binding and bending DNA via both sequence-specific and sequence non-specific modes. All HMG proteins are subjected to extensive post-translational modifications (PTMs) like phosphorylation, acetylation, methylation, etc. In this work, we propose to understand how PTMs (or the associated PTM-mimicking mutations) can modulate folding mechanism, thermodynamic stability, and the strength of DNA binding for a selection of sequence non-specific HMG proteins with either a single (Nhp6A, Nhp6B) or two HMG-motifs through multi-probe spectroscopy. It is also being increasingly recognized that liquid-liquid phase separation (LLPS) or biomolecular condensate formation can potentially act as a genome packaging/sequestering mechanism for many DNA-associated proteins involved in chromatin remodeling. We therefore plan to further study the formation or dissolution of biomolecular condensates (if any), and to understand the crosstalk between PTMs and phase separation of yeast HMGs with DNA.