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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 34 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 solutions viscosity (intrinsic viscosity of unfolded proteins increases with increase in molecular mass)

Dehydrated or barrier-compromised skin

Khan, F.Y., et al

If your research protocol needs more than one vial, mention it when placing your peptide order and we'll do our best to include extra vials as a courtesy, depending on order size