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Pattern formation in drying protein droplets continues to attractconsiderable research attention because it can be linked to specificprotein-protein interactions. An extensive study of the drying evolution andthe final crack patterns are presented, highlighting the concentrationdependence (from 1 to 13 wt%) on two globular proteins, lysozyme (Lys) andbovine serum albumin (BSA), in de-ionized water. The drying evolution startswith a constant contact radius mode and shifts to a mixed mode where both fluidfront and contact angle changes. The contact angle monotonically decreases,whereas, the fluid front exhibits two regimes: an initial linear regime and alater nonlinear regime. Unlike the linear regime, the non-linear regime isfaster for Lys droplets. This results in the formation of a "mound"-likestructure in the central region. A new feature, a "dimple" is observed in thismound which is found to be dependent on the initial concentration. Thedifferent crack morphology of BSA and Lys depends strongly on the initial stateof the solution and can be interpreted using a simple mechanical model. Infact, when dried under uniform conditions (surface, humidity, temperature,droplet diameter, etc.), the evolution and the final pattern displays as afingerprint of the initial state.

A Comparative Study of the Drying Evolution and Dried Morphology of two Globular Protein and De-ionized water Solutions