Date Approved

1-26-2024

Embargo Period

1-26-2024

Document Type

Thesis

Degree Name

Master of Science (M.S.) Bioinformatics

Department

Molecular and Cellular Biosciences

College

College of Science & Mathematics

Advisor

Benjamin Carone, Ph.D.

Committee Member 1

Nathaniel Nucci, Ph.D.

Committee Member 2

Chun Wu, Ph.D.

Keywords

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

Subject(s)

Cytoskeletal proteins--Analysis

Disciplines

Biochemistry, Biophysics, and Structural Biology | Bioinformatics

Abstract

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.

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