Iannacchione, Germano S.
Stroe, Izabela RC
The fundamental interactions between proteins and liquid crystals were studied using 4-Cyano-4'-pentylbiphenyl (5CB) and equine heart myoglobin in varying concentrations. Polarizing Light Microscopy was used to capture images of pure and mixed components, depicting a caging process of the 5CB by the myoglobin as it competes for interaction with water. Dielectric Relaxation Spectroscopy and Differential Scanning Calorimetry provided evidence of an inverse relationship between the hydrated-myoglobin/5CB ratio and charge carrier diffusion barrier energy and nematic-isotropic transition temperature respectively. A trend in the heat capacitance peak shift alludes to an additional process related to a possible optimum concentration, which correlates with the microscopy caging process analysis.
Worcester Polytechnic Institute
Major Qualifying Project
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