Infrared Microspectroscopy study of insulin crystals at high pressure

During the last years the coupling of high pressure techniques and infrared spectroscopy has proven to be a very powerful tool in the study of conformational changes of proteins. Protein unfolding and monomerization are events that are expected to take place at high pressure due to the peculiarity of pressure to shift the system towards the state that occupies the minimum volume. We observed the growth of apparently cubic crystals at a pressure of about 4 kbar, subjecting to high pressure a solution of misfolded insulin. Even if high pressure is commonly used to tune the growth rate of crystals, protein crystallization at high pressure is not a well known process and no evidences of the particular case of insulin are present in literature.