Our research is focused on understanding how protein-protein interactions influence thermodynamics in biological systems. Proteins are polymers composed of unique sequences of amino acid monomers. The variety of amino acids available allows for many potential types of protein-protein interactions that can catalyze chemical reactions in cells and build biological structures to support load. A human being functions properly because proteins interact uniquely with one another.

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• Dynamics of peptide aggregation
• Equilibrium properties of peptide aggregates
  
• Dynamics of peptide gels
• Proteins in a cellular environment

• BSE 3154
• BSE 3504
• BSE 4514
• BSE 5644
• ENGR 3124
• EPA P3

G. Farrar, J. Barone, A. Morgan, “Creation of ovalbumin based porous scaffolds for bone tissue regeneration,” submitted to J. Tissue Eng.

Z. Li, S.H. Renneckar, and J.R. Barone, “Polyphenol-nanocellulose nanocomposites that biomimic the plant cell wall,” Cellulose, 17, 57-68 (2010).

J.R. Barone, “Lignocellulosic fiber-reinforced keratin polymer composites,” Journal of Polymers and the Environment, 17, 143-151 (2009).

A. Athamneh and J.R. Barone, “Enzyme-mediated self-assembly of highly ordered structures from disordered proteins,”Smart Materials and Structures, 18, 104024 (2009).

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