Intrinsically disordered proteins (IDPs), essential for regulating critical cellular functions, have long posed research challenges due to their lack of fixed three-dimensional structure. They are now more accessible for study thanks to a new model that enables rapid and precise analysis of their hydrodynamic properties, marking a significant breakthrough in biophysical research. In recent years, the significance of intrinsically disordered proteins (IDPs) in cellular processes has become increasingly apparent. These proteins, often referred to as the "dark matter of molecular biology", play crucial roles in processes such as gene expression regulation and biomineralization. Unlike proteins with stable three-dimensional structures, IDPs lack a defined shape, which allows them to perform various functions in response to changing cellular conditions. However, this structural flexibility makes them challenging to study, particularly when it comes to predicting their hydrodynamic properties, which are necessary for understanding their biological roles. The hydrodynamic radius (Rh), which represents the radius of a hypothetical sphere moving in the solvent like the protein molecule, is the most critical parameter in describing a protein's movement in solution. For structured proteins, the hydrodynamic radius can be predicted with high accuracy based on their mass or chain length. However, this approach fails for disordered proteins, as traditional methods for estimating Rh either fall short or are computationally too complex to be practical, especially for long-chain IDPs. To address this challenge, a research team at the Environmental Laboratory of Biological Physics, led by Anna Niedźwiecka and in collaboration with Piotr Szymczak's theoretical group from the University of Warsaw, has developed a new model for disordered proteins specifically tailored for estimating Rh. This model employs accelerated conformational sampling through a self-avoiding random walk, accounts for hydrodynamic interactions between coarse-grained protein subunits, and quickly calculates the hydrodynamic radius based on minimal scattering approximation. This allows for accurate predictions of Rh based solely on the protein sequence, making it a new and effective tool for scientists. In a recent paper published in the Journal of Physical Chemistry Letters, the authors also presented results of testing on a range of new protein constructs that varied significantly in chain length and content of globular domains and disordered linkers. They measured their hydrodynamic radii using fluorescence correlation spectroscopy and demonstrated good agreement between their calculations and experimental results. This work provides the most comprehensive set of experimental data available for such studies. The new model not only provides Rh estimates within seconds but also achieves better accuracy than previous coarse-grained or phenomenological computational methods. The new method for predicting hydrodynamic properties based solely on protein sequence will impact both biophysical research and potential biomedical applications, where understanding the behavior of disordered proteins is crucial.