Date Approved


Embargo Period


Document Type


Degree Name

Master of Science (M.S.) Bioinformatics


Molecular and Cellular Biosciences


College of Science & Mathematics


Benjamin Carone, Ph.D.

Committee Member 1

Nathaniel Nucci, Ph.D.

Committee Member 2

Chun Wu, Ph.D.


elastin-like polypeptides; intrinsically disordered proteins, physical properties of structural proteins


Cytoskeletal proteins--Analysis


Biochemistry, Biophysics, and Structural Biology | Bioinformatics


The elastin-like polypeptide (ELP) is a well-studied structural protein that is easily amenable to amino acid (AA) sequence modifications and has the potential to yield a wide variety of uses in bioengineering and biomedical applications. One unique property of ELP is the inclusion of intrinsically disordered domains (IDP) within the structure that allow for its diversity of physical properties. While it is generally understood that amino acid sequence dictates protein folding arrangements, the contributions of specific amino acid sequences to the intrinsic disorder of ELP has yet to be fully resolved. Therefore, identifying the contributions of specific amino acid sequences to the final physical properties of ELP at the sequence level is an important step in understanding the basis of ELP’s unique biophysical properties. The results of this study resolve the role of amino acid sequence and repeat composition on the disordered structure of ELP. Experimentally, an enhanced synthetic ELP[AV-60] was developed, produced, and purified, with novel photocrosslinking and a transition temperature of 37°C. Computationally, the conserved AA sequence of valine-proline (VP) in the endogenous ELN sequence and its major function in the structure of ELP was identified. Finally, we identified a specific AA monomeric unit, VPGXAG with potential for application in IDPs research.