Graduate Thesis Or Dissertation
 

Surface tension kinetics of the wild type and four synthetic, structural stability mutants of bacteriophage T4 lysozyme at the air-water interface

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  • Surface tension kinetics exhibited by selected stability mutants of T4 lysozyme at the air-water interface were monitored with DuNoüy tensiometry. Mutant lysozymes were produced by substitution of isoleucine at position 3 with cysteine, leucine, tryptophan and glycine. Each substitution resulted in an altered structural stability quantified by a change in the free energy of unfolding. At a bulk concentration of 1.0 mg/ml, an analysis of surface tension kinetics using first-order rate equations yielded two rate constants, reflecting protein surface hydrophobicity and molecular weight, respectively. These rate constants varied little among the five T4 lysozyme variants. At a bulk concentration of 0.01 mg/ml, the same analysis gave one rate constant that correlated with protein structural stability. Additionally, the surface pressure kinetics were compared to the kinetic model evolving from a simple model for protein adsorption. This model allowed for parallel, irreversible adsorption into two states directly from solution, where state 2 molecules were more tightly bound to the surface and occupied greater interfacial area than state I molecules. The model indicated that less stable variants of T4 lysozyme have a greater tendency to adsorb in state 2, and state 2 molecules increase spreading pressure more than state 1 molecules occupying the same interfacial area. This phenomenon is more pronounced at lower concentration than at higher concentration.
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