This CG potential was introduced in 2010 ( ) for the study of DNA systems. It was later expanded to protein systems and in the last version, SIRAH 2.0 is able to describe metal ion coordination, unbiased conformational sampling for free energy calculations, and specific protein-peptide recognition . This CG model was developed following a top-down approach that fits interactions to structural data from sources like the PDB and canonical structures such as B-DNA, 𝛼-helices, and 𝛽-peptides. It avoids using specific algorithms for parameter development, allowing flexibility through trial-and-error to enhance resolution in key areas. Unlike other CG potentials, SIRAH is unbiased, avoiding artificial constraints on secondary structures. Partial charges on each bead create a dipole moment, enabling dielectric permittivity and permits tuning of the ionic strength of the solution, inducing ion-specific DNA molecule that align with high-resolution structures. The study of the single chain conformational ensembles of an intrinsically disordered protein (IDP) in SIRAH (80) matched well with the NMR conformers. However, reproducing single chain properties is not sufficient for interpretation of the phase diagram in protein condensates , in particular when no switching of transient secondary protein structures in CG simulations (e.g. 𝛽, 𝛼 and coil and between themselves) is yet capture. Those conformational changes are key for the stabilization of protein condensates transitioning to the aberrant phase (e.g. 𝛽-amyloid fibrils) and still faces real challenges . Martins and Galamba recently employed SIRAH for the study of the monomer and small oligomers of 𝛼-synuclein . Due to the high resolution of the SIRAH protein backbone (i.e. N-C𝛼-O), the model reproduced 𝑅 𝑔 values in the range of ≈ 2nm according to all-atom MD simulations generated by Amber99sb and Charmm36m. However, SIRAH model has not yet been used to explore protein condensates and careful interpretation should be done in case of capturing single-molecule properties of IDPs for prediction of biomolecular phase diagrams . Robles et al. investigated the conformational changes associated with activation or inactivation by an agonist (p-TA) and antagonists (EPPTB and RTI) in the human trace amine-associated receptor (hTAAR1), which is a G protein-coupled receptor. Elucidating the mechanics of activation can play a role in the developed of a treatment of neuropsychiatric condition. CG simulations confirmed in time time scale of 5𝜇s that G protein interacts with intracellular loop 3 (ICL3) as well as with intracellular segments of several TMDs. Agonist binding promotes compact receptor conformations associated with activation, whereas antagonists stabilize the receptor in an inactive state. These findings illuminate the dynamic nature of GPCR modulation and the critical role of ICL3 movement in receptor signaling. The CG potentials, simulation tools and parameters can be accessed freely from the webpage ()