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These and many other early experiments that used viscometry to study protein denaturation and unfolding laid the groundwork for understanding intrinsically disordered states by showing that a rigid, compact, globular protein has a small effect on viscosity because it occupies a small hydrodynamic volume (they typically have a low intrinsic viscosity, in the range of 3–4 mL/g, which is independent of protein molecular mass), whereas an unfolded, flexible, or disordered protein adopts a random coil-like conformation, creating a much larger hydrodynamic volume that increases the solution’s viscosity (intrinsic viscosity of unfolded proteins increases with increase in molecular mass)