Faculty Advisor

Iannacchione, Germano S.

Faculty Advisor

Stroe, Izabela RC

Abstract

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.

Publisher

Worcester Polytechnic Institute

Date Accepted

April 2013

Major

Physics

Project Type

Major Qualifying Project

Accessibility

Unrestricted

Advisor Department

Physics

Advisor Program

Physics

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